A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 1.11.1.9.
A glutathione transferase that catalyzes the conjugation of electrophilic substrates to GLUTATHIONE. This enzyme has been shown to provide cellular protection against redox-mediated damage by FREE RADICALS.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.
The rate dynamics in chemical or physical systems.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A species of the true toads, Bufonidae, widely distributed in the United States and Europe.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion.
A superorder in the class CEPHALOPODA, consisting of the orders Octopoda (octopus) with over 200 species and Vampyromorpha with a single species. The latter is a phylogenetic relic but holds the key to the origins of Octopoda.
A derivative of ACETIC ACID that contains two CHLORINE atoms attached to its methyl group.
Mixture of 2- and 3-tert-butyl-4-methoxyphenols that is used as an antioxidant in foods, cosmetics, and pharmaceuticals.
A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.
One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.3.
A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.
**Maleates** are organic compounds that contain a carboxylic acid group and a hydroxyl group attached to adjacent carbon atoms, often used as intermediates in the synthesis of pharmaceuticals and other chemicals, or as drugs themselves, such as maleic acid or its salts.
Compounds containing the -SH radical.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A compound that inhibits symport of sodium, potassium, and chloride primarily in the ascending limb of Henle, but also in the proximal and distal tubules. This pharmacological action results in excretion of these ions, increased urinary output, and reduction in extracellular fluid. This compound has been classified as a loop or high ceiling diuretic.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria that is frequently isolated from clinical specimens. Its most common site of infection is the urinary tract.
Unsaturated hydrocarbons of the type Cn-H2n, indicated by the suffix -ene. (Grant & Hackh's Chemical Dictionary, 5th ed, p408)
A sulfur-containing alkyl thionitrite that is one of the NITRIC OXIDE DONORS.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
A synthetic amino acid that depletes glutathione by irreversibly inhibiting gamma-glutamylcysteine synthetase. Inhibition of this enzyme is a critical step in glutathione biosynthesis. It has been shown to inhibit the proliferative response in human T-lymphocytes and inhibit macrophage activation. (J Biol Chem 1995;270(33):1945-7)
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Organic compounds with the general formula R-NCS.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A non-selective post-emergence, translocated herbicide. According to the Seventh Annual Report on Carcinogens (PB95-109781, 1994) this substance may reasonably be anticipated to be a carcinogen. (From Merck Index, 12th ed) It is an irreversible inhibitor of CATALASE, and thus impairs activity of peroxisomes.
Organic compounds containing a carbonyl group in the form -CHO.
Proteins prepared by recombinant DNA technology.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
Naturally occurring or synthetic substances that inhibit or retard the oxidation of a substance to which it is added. They counteract the harmful and damaging effects of oxidation in animal tissues.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
Organic compounds composed of tin and three ethyl groups. Affect mitochondrial metabolism and inhibit oxidative phosphorylation by acting directly on the energy conserving processes.
Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.
Butanones, also known as methyl ethyl ketone or MEK, are organic compounds consisting of a four-carbon chain with a ketone functional group located at the second carbon atom, classified as dimethyl ketones, and commonly used in industrial and laboratory settings as solvents and chemical intermediates.
A chlorinated hydrocarbon that has been used as an inhalation anesthetic and acts as a narcotic in high concentrations. Its primary use is as a solvent in manufacturing and food technology.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
Iodinated hydrocarbons are organic compounds containing carbon and hydrogen atoms, with iodine atoms covalently bonded to them, which are used in medical imaging as radiocontrast agents.
Peroxides produced in the presence of a free radical by the oxidation of unsaturated fatty acids in the cell in the presence of molecular oxygen. The formation of lipid peroxides results in the destruction of the original lipid leading to the loss of integrity of the membranes. They therefore cause a variety of toxic effects in vivo and their formation is considered a pathological process in biological systems. Their formation can be inhibited by antioxidants, such as vitamin E, structural separation or low oxygen tension.
Organometallic compounds which contain tin and three alkyl groups.
Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.
'Nitrobenzenes' are organic compounds characterized by the presence of a nitro group (-NO2) attached to a benzene ring, with the molecular formula C6H5NO2, which can be hazardous and toxic, and have various applications in industry, such as solvents, dyes, and explosives.
A reagent that is highly selective for the modification of arginyl residues. It is used to selectively inhibit various enzymes and acts as an energy transfer inhibitor in photophosphorylation.
A group of compounds that are derivatives of methoxybenzene and contain the general formula R-C7H7O.
An enzyme that catalyzes the interconversion of methylglyoxal and lactate, with glutathione serving as a coenzyme. EC 4.4.1.5.
A non-template-directed DNA polymerase normally found in vertebrate thymus and bone marrow. It catalyzes the elongation of oligo- or polydeoxynucleotide chains and is widely used as a tool in the differential diagnosis of acute leukemias in man. EC 2.7.7.31.
A chelating agent that has been used to mobilize toxic metals from the tissues of humans and experimental animals. It is the main metabolite of DISULFIRAM.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.
Any of the monobasic inorganic or organic acids of sulfur with the general formula RSO(OH). (From McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)
Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. Enzymes in this group are instrumental in ketone body metabolism and utilization of acetoacetate in mitochondria. EC 2.8.3.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Experimentally induced tumors of the LIVER.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
(2S-(2 alpha,3 beta(1E,3E,5Z,8Z)))-3-(1,3,5,8-Tetradecatetraenyl)oxiranebutanoic acid. An unstable allylic epoxide, formed from the immediate precursor 5-HPETE via the stereospecific removal of a proton at C-10 and dehydration. Its biological actions are determined primarily by its metabolites, i.e., LEUKOTRIENE B4 and cysteinyl-leukotrienes. Alternatively, leukotriene A4 is converted into LEUKOTRIENE C4 by glutathione-S-transferase or into 5,6-di-HETE by the epoxide-hydrolase. (From Dictionary of Prostaglandins and Related Compounds, 1990)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A phenolphthalein that is used as a diagnostic aid in hepatic function determination.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
INDOLES which have two keto groups forming QUINONES like structures of the indole aromatic ring.
Pigment obtained by the oxidation of epinephrine.
Chemical substances that are foreign to the biological system. They include naturally occurring compounds, drugs, environmental agents, carcinogens, insecticides, etc.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
7,8,8a,9a-Tetrahydrobenzo(10,11)chryseno (3,4-b)oxirene-7,8-diol. A benzopyrene derivative with carcinogenic and mutagenic activity.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations.
The pH in solutions of proteins and related compounds at which the dipolar ions are at a maximum.
An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 1.15.1.1.
Methionine Sulfoximine is a toxic compound that functions as an inhibitor of methionine metabolism, being formed through the oxidation of methionine by the enzyme methionine sulfoxide reductase.
Organic compounds that contain 1,2-diphenylethylene as a functional group.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Organic derivatives of thiocyanic acid which contain the general formula R-SCN.
A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES).
Technique involving the diffusion of antigen or antibody through a semisolid medium, usually agar or agarose gel, with the result being a precipitin reaction.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.
A sulfhydryl reagent that is widely used in experimental biochemical studies.
Surgical removal or destruction of the hypophysis, or pituitary gland. (Dorland, 28th ed)
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Diminished or failed response of an organism, disease or tissue to the intended effectiveness of a chemical or drug. It should be differentiated from DRUG TOLERANCE which is the progressive diminution of the susceptibility of a human or animal to the effects of a drug, as a result of continued administration.
A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.
A carcinogen that is often used in experimental cancer studies.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
Established cell cultures that have the potential to propagate indefinitely.
A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
The sum of the weight of all the atoms in a molecule.
A method of gel filtration chromatography using agarose, the non-ionic component of agar, for the separation of compounds with molecular weights up to several million.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.
Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
An element with the atomic symbol Se, atomic number 34, and atomic weight 78.96. It is an essential micronutrient for mammals and other animals but is toxic in large amounts. Selenium protects intracellular structures against oxidative damage. It is an essential component of GLUTATHIONE PEROXIDASE.
The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.
Substances that increase the risk of NEOPLASMS in humans or animals. Both genotoxic chemicals, which affect DNA directly, and nongenotoxic chemicals, which induce neoplasms by other mechanism, are included.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
The development by insects of resistance to insecticides.
Measurement of the intensity and quality of fluorescence.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS.
Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
Enzymes of the isomerase class that catalyze the oxidation of one part of a molecule with a corresponding reduction of another part of the same molecule. They include enzymes converting aldoses to ketoses (ALDOSE-KETOSE ISOMERASES), enzymes shifting a carbon-carbon double bond (CARBON-CARBON DOUBLE BOND ISOMERASES), and enzymes transposing S-S bonds (SULFUR-SULFUR BOND ISOMERASES). (From Enzyme Nomenclature, 1992) EC 5.3.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.
An enzyme that catalyzes the synthesis of geranylgeranyl diphosphate from trans, trans-farnesyl diphosphate and isopentenyl diphosphate.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
The N-acetyl derivative of CYSTEINE. It is used as a mucolytic agent to reduce the viscosity of mucous secretions. It has also been shown to have antiviral effects in patients with HIV due to inhibition of viral stimulation by reactive oxygen intermediates.
The resistance that a gaseous or liquid system offers to flow when it is subjected to shear stress. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
A genus of mosquitoes (CULICIDAE) that are known vectors of MALARIA.
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
F344 rats are an inbred strain of albino laboratory rats (Rattus norvegicus) that have been widely used in biomedical research due to their consistent and reliable genetic background, which facilitates the study of disease mechanisms and therapeutic interventions.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
Elements of limited time intervals, contributing to particular results or situations.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The genetic constitution of the individual, comprising the ALLELES present at each GENETIC LOCUS.
The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
The regular and simultaneous occurrence in a single interbreeding population of two or more discontinuous genotypes. The concept includes differences in genotypes ranging in size from a single nucleotide site (POLYMORPHISM, SINGLE NUCLEOTIDE) to large nucleotide sequences visible at a chromosomal level.
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
A pair of glands located at the cranial pole of each of the two KIDNEYS. Each adrenal gland is composed of two distinct endocrine tissues with separate embryonic origins, the ADRENAL CORTEX producing STEROIDS and the ADRENAL MEDULLA producing NEUROTRANSMITTERS.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
The dialdehyde of malonic acid.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.

The role of gene splicing, gene amplification and regulation in mosquito insecticide resistance. (1/8048)

The primary routes of insecticide resistance in all insects are alterations in the insecticide target sites or changes in the rate at which the insecticide is detoxified. Three enzyme systems, glutathione S-transferases, esterases and monooxygenases, are involved in the detoxification of the four major insecticide classes. These enzymes act by rapidly metabolizing the insecticide to non-toxic products, or by rapidly binding and very slowly turning over the insecticide (sequestration). In Culex mosquitoes, the most common organophosphate insecticide resistance mechanism is caused by co-amplification of two esterases. The amplified esterases are differentially regulated, with three times more Est beta 2(1) being produced than Est alpha 2(1). Cis-acting regulatory sequences associated with these esterases are under investigation. All the amplified esterases in different Culex species act through sequestration. The rates at which they bind with insecticides are more rapid than those for their non-amplified counterparts in the insecticide-susceptible insects. In contrast, esterase-based organophosphate resistance in Anopheles is invariably based on changes in substrate specificities and increased turnover rates of a small subset of insecticides. The up-regulation of both glutathione S-transferases and monooxygenases in resistant mosquitoes is due to the effects of a single major gene in each case. The products of these major genes up-regulate a broad range of enzymes. The diversity of glutathione S-transferases produced by Anopheles mosquitoes is increased by the splicing of different 5' ends of genes, with a single 3' end, within one class of this enzyme family. The trans-acting regulatory factors responsible for the up-regulation of both the monooxygenase and glutathione S-transferases still need to be identified, but the recent development of molecular tools for positional cloning in Anopheles gambiae now makes this possible.  (+info)

Detailed methylation analysis of the glutathione S-transferase pi (GSTP1) gene in prostate cancer. (2/8048)

Glutathione-S-Transferases (GSTs) comprise a family of isoenzymes that provide protection to mammalian cells against electrophilic metabolites of carcinogens and reactive oxygen species. Previous studies have shown that the CpG-rich promoter region of the pi-class gene GSTP1 is methylated at single restriction sites in the majority of prostate cancers. In order to understand the nature of abnormal methylation of the GSTP1 gene in prostate cancer we undertook a detailed analysis of methylation at 131 CpG sites spanning the promoter and body of the gene. Our results show that DNA methylation is not confined to specific CpG sites in the promoter region of the GSTP1 gene but is extensive throughout the CpG island in prostate cancer cells. Furthermore we found that both alleles are abnormally methylated in this region. In normal prostate tissue, the entire CpG island was unmethylated, but extensive methylation was found outside the island in the body of the gene. Loss of GSTP1 expression correlated with DNA methylation of the CpG island in both prostate cancer cell lines and cancer tissues whereas methylation outside the CpG island in normal prostate tissue appeared to have no effect on gene expression.  (+info)

The abundance of cell cycle regulatory protein Cdc4p is controlled by interactions between its F box and Skp1p. (3/8048)

Posttranslational modification of a protein by ubiquitin usually results in rapid degradation of the ubiquitinated protein by the proteasome. The transfer of ubiquitin to substrate is a multistep process. Cdc4p is a component of a ubiquitin ligase that tethers the ubiquitin-conjugating enzyme Cdc34p to its substrates. Among the domains of Cdc4p that are crucial for function are the F-box, which links Cdc4p to Cdc53p through Skp1p, and the WD-40 repeats, which are required for binding the substrate for Cdc34p. In addition to Cdc4p, other F-box proteins, including Grr1p and Met30p, may similarly act together with Cdc53p and Skp1p to function as ubiquitin ligase complexes. Because the relative abundance of these complexes, known collectively as SCFs, is important for cell viability, we have sought evidence of mechanisms that modulate F-box protein regulation. Here we demonstrate that the abundance of Cdc4p is subject to control by a peptide segment that we term the R-motif (for "reduced abundance"). Furthermore, we show that binding of Skp1p to the F-box of Cdc4p inhibits R-motif-dependent degradation of Cdc4p. These results suggest a general model for control of SCF activities.  (+info)

Physical interaction of the bHLH LYL1 protein and NF-kappaB1 p105. (4/8048)

The LYL1 gene was first identified upon the molecular characterization of the t(7;9)(q35;p13) translocation associated with some human T-cell acute leukemias (T-ALLs). In adult tissues, LYL1 expression is restricted to hematopoietic cells with the notable exclusion of the T cell lineage. LYL1 encodes a basic helix-loop-helix (bHLH) protein highly related to TAL-1, whose activation is also associated with a high proportion of human T-ALLs. A yeast two-hybrid system was used to identify proteins that specifically interact with LYL1 and might mediate its activities. We found that p105, the precursor of NF-kappaB1 p50, was the major LYL1-interacting protein in this system. The association between LYL1 and p105 was confirmed both in vitro and in vivo in mammalian cells. Biochemical studies indicated that the interaction was mediated by the bHLH motif of LYL1 and the ankyrin-like motifs of p105. Ectopic expression of LYL1 in a human T cell line caused a significant decrease in NF-kappaB-dependent transcription, associated with a reduced level of NF-kappaB1 proteins.  (+info)

Co-expression of glutathione S-transferase with methionine aminopeptidase: a system of producing enriched N-terminal processed proteins in Escherichia coli. (5/8048)

We describe here an Escherichia coli expression system that produces recombinant proteins enriched in the N-terminal processed form, by using glutathione S-transferase cGSTM1-1 and rGSTT1-1 as models, where c and r refer to chick and rat respectively. Approximately 90% of the cGSTM1-1 or rGSTT1-1 overexpressed in E. coli under the control of a phoA promoter retained the initiator methionine residue that was absent from the mature isoenzymes isolated from tissues. The amount of initiator methionine was decreased to 40% of the expressed cGSTM1-1 when the isoenzyme was co-expressed with an exogenous methionine aminopeptidase gene under the control of a separate phoA promoter. The recombinant proteins expressed were mainly methionine aminopeptidase. The yield of cGSTM1-1 was decreased to 10% of that expressed in the absence of the exogenous methionine aminopeptidase gene. By replacing the phoA with its natural promoter, the expression of methionine aminopeptidase decreased drastically. The yield of the co-expressed cGSTM1-1 was approx. 60% of that in the absence of the exogenous methionine aminopeptidase gene; approx. 65% of the initiator methionine residues were removed from the enzyme. Under similar conditions, N-terminal processing was observed in approx. 70% of the recombinant rGSTT1-1 expressed. By increasing the concentration of phosphate in the growth medium, the amount of initiator methionine on cGSTM1-1 was decreased to 14% of the overexpressed isoenzymes, whereas no further improvement could be observed for rGSTT1-1. The initiator methionine residue does not affect the enzymic activities of either cGSTM1-1 or rGSTT1-1. However, the epoxidase activity and the 4-nitrobenzyl chloride-conjugating activity of the purified recombinant rGSTT1-1 are markedly higher that those reported recently for the same isoenzyme isolated from rat livers.  (+info)

Oval cell numbers in human chronic liver diseases are directly related to disease severity. (6/8048)

The risk of developing hepatocellular carcinoma is significantly increased in patients with genetic hemochromatosis, alcoholic liver disease, or chronic hepatitis C infection. The precise mechanisms underlying the development of hepatocellular carcinoma in these conditions are not well understood. Stem cells within the liver, termed oval cells, are involved in the pathogenesis of hepatocellular carcinoma in animal models and may be important in the development of hepatocellular carcinoma in human chronic liver diseases. The aims of this study were to determine whether oval cells could be detected in the liver of patients with genetic hemochromatosis, alcoholic liver disease, or chronic hepatitis C, and whether there is a relationship between the severity of the liver disease and the number of oval cells. Oval cells were detected using histology and immunohistochemistry in liver biopsies from patients with genetic hemochromatosis, alcoholic liver disease, or chronic hepatitis C. Oval cells were not observed in normal liver controls. Oval cell numbers increased significantly with the progression of disease severity from mild to severe in each of the diseases studied. We conclude that oval cells are frequently found in subjects with genetic hemochromatosis, alcoholic liver disease, or chronic hepatitis C. There is an association between severity of liver disease and increase in the number of oval cells consistent with the hypothesis that oval cell proliferation is associated with increased risk for development of hepatocellular carcinoma in chronic liver disease.  (+info)

Susceptibility to childhood acute lymphoblastic leukemia: influence of CYP1A1, CYP2D6, GSTM1, and GSTT1 genetic polymorphisms. (7/8048)

Although acute lymphoblastic leukemia (ALL) is the most common childhood cancer, factors governing susceptibility to this disease have not yet been identified. As such, ALL offers a useful opportunity to examine the glutathione S-transferase and cytochrome P450 genes in determining susceptibility to pediatric cancers. Both enzymes are involved in carcinogen metabolism and have been shown to influence the risk a variety of solid tumors in adults. To determine whether these genes played a similar role in childhood leukemogenesis, we compared the allele frequencies of 177 childhood ALL patients and 304 controls for the CYP1A1, CYP2D6, GSTM1, and GSTT1 genes. We chose the French population of Quebec as our study population because of its relative genetic homogeneity. The GSTM1 null and CYP1A1*2A genotypes were both found to be significant predictors of ALL risk (odds ratio [OR] = 1.8). Those possessing both genotypes were at an even greater risk of developing the disease (OR = 3.3). None of the other alleles tested for proved to be significant indicators of ALL risk. Unexpectedly, girls carrying the CYP1A1*4 were significantly underrepresented in the ALL group (OR = 0.2), suggesting that a gender-specific protective role exists for this allele. These results suggest that the risk of ALL may indeed be associated with xenobiotics-metabolism, and thus with environmental exposures. Our findings may also explain, in part, why ALL is more prevalent among males than females.  (+info)

Combining SSH and cDNA microarrays for rapid identification of differentially expressed genes. (8/8048)

Comparing patterns of gene expression in cell lines and tissues has important applications in a variety of biological systems. In this study we have examined whether the emerging technology of cDNA microarrays will allow a high throughput analysis of expression of cDNA clones generated by suppression subtractive hybridization (SSH). A set of cDNA clones including 332 SSH inserts amplified by PCR was arrayed using robotic printing. The cDNA arrays were hybridized with fluorescent labeled probes prepared from RNA from ER-positive (MCF7 and T47D) and ER-negative (MDA-MB-231 and HBL-100) breast cancer cell lines. Ten clones were identified that were over-expressed by at least a factor of five in the ER-positive cell lines. Northern blot analysis confirmed over-expression of these 10 cDNAs. Sequence analysis identified four of these clones as cytokeratin 19, GATA-3, CD24 and glutathione-S-transferase mu-3. Of the remaining six cDNA clones, four clones matched EST sequences from two different genes and two clones were novel sequences. Flow cytometry and immunofluorescence confirmed that CD24 protein was over-expressed in the ER-positive cell lines. We conclude that SSH and microarray technology can be successfully applied to identify differentially expressed genes. This approach allowed the identification of differentially expressed genes without the need to obtain previously cloned cDNAs.  (+info)

Glutathione transferases (GSTs) are a group of enzymes involved in the detoxification of xenobiotics and endogenous compounds. They facilitate the conjugation of these compounds with glutathione, a tripeptide consisting of cysteine, glutamic acid, and glycine, which results in more water-soluble products that can be easily excreted from the body.

GSTs play a crucial role in protecting cells against oxidative stress and chemical injury by neutralizing reactive electrophilic species and peroxides. They are found in various tissues, including the liver, kidneys, lungs, and intestines, and are classified into several families based on their structure and function.

Abnormalities in GST activity have been associated with increased susceptibility to certain diseases, such as cancer, neurological disorders, and respiratory diseases. Therefore, GSTs have become a subject of interest in toxicology, pharmacology, and clinical research.

Glutathione is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It is a vital antioxidant that plays an essential role in maintaining cellular health and function. Glutathione helps protect cells from oxidative stress by neutralizing free radicals, which are unstable molecules that can damage cells and contribute to aging and diseases such as cancer, heart disease, and dementia. It also supports the immune system, detoxifies harmful substances, and regulates various cellular processes, including DNA synthesis and repair.

Glutathione is found in every cell of the body, with particularly high concentrations in the liver, lungs, and eyes. The body can produce its own glutathione, but levels may decline with age, illness, or exposure to toxins. As such, maintaining optimal glutathione levels through diet, supplementation, or other means is essential for overall health and well-being.

Dinitrochlorobenzene (DNCB) is a chemical compound that is classified as an aromatic organic compound. Its medical definition relates to its use as a topical immunotherapy for the treatment of certain skin conditions. DNCB is a potent sensitizer and hapten, which means that it can cause an immune response when it comes into contact with the skin.

When applied to the skin, DNCB can stimulate the production of antibodies and activate immune cells, leading to an inflammatory reaction. This property has been exploited in the treatment of conditions such as alopecia areata, a type of hair loss that is thought to be caused by an autoimmune response. By sensitizing the patient's immune system to DNCB, it may be possible to modulate the immune response and promote hair growth.

However, the use of DNCB as a therapeutic agent is not without risks. It can cause significant local reactions, including redness, swelling, and blistering, and there is a risk of systemic toxicity if it is absorbed into the bloodstream. As such, its use is generally restricted to specialized medical settings where it can be administered under close supervision.

Glutathione peroxidase (GPx) is a family of enzymes with peroxidase activity whose main function is to protect the organism from oxidative damage. They catalyze the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxides to water or corresponding alcohols, using glutathione (GSH) as a reducing agent, which is converted to its oxidized form (GSSG). There are several isoforms of GPx found in different tissues, including GPx1 (also known as cellular GPx), GPx2 (gastrointestinal GPx), GPx3 (plasma GPx), GPx4 (also known as phospholipid hydroperoxide GPx), and GPx5-GPx8. These enzymes play crucial roles in various biological processes, such as antioxidant defense, cell signaling, and apoptosis regulation.

Glutathione S-transferase Pi (GSTP1) is a member of the glutathione S-transferase (GST) family, which are enzymes involved in the detoxification of xenobiotics and endogenous compounds. GSTs catalyze the conjugation of reduced glutathione to these electrophilic compounds, facilitating their excretion from the body.

GSTP1 is primarily found in the cytosol of cells and has a high affinity for a variety of substrates, including polycyclic aromatic hydrocarbons, heterocyclic amines, and certain chemotherapeutic drugs. It plays an essential role in protecting cells against oxidative stress and chemical-induced damage.

Polymorphisms in the GSTP1 gene have been associated with altered enzyme activity and susceptibility to various diseases, including cancer, neurological disorders, and respiratory diseases. The most common polymorphism in GSTP1 is a single nucleotide substitution (Ile105Val), which has been shown to reduce the enzyme's catalytic activity and increase the risk of developing certain types of cancer.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Glutathione reductase (GR) is an enzyme that plays a crucial role in maintaining the cellular redox state. The primary function of GR is to reduce oxidized glutathione (GSSG) to its reduced form (GSH), which is an essential intracellular antioxidant. This enzyme utilizes nicotinamide adenine dinucleotide phosphate (NADPH) as a reducing agent in the reaction, converting it to NADP+. The medical definition of Glutathione Reductase is:

Glutathione reductase (GSR; EC 1.8.1.7) is a homodimeric flavoprotein that catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH) in the presence of NADPH as a cofactor. This enzyme is essential for maintaining the cellular redox balance and protecting cells from oxidative stress by regenerating the active form of glutathione, a vital antioxidant and detoxifying agent.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Glutathione disulfide (GSSG) is the oxidized form of glutathione (GSH), which is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It plays a crucial role in maintaining cellular redox homeostasis by scavenging free radicals and reactive oxygen species (ROS) in the body.

Glutathione exists in two forms - reduced (GSH) and oxidized (GSSG). In the reduced form, glutathione has a sulfhydryl group (-SH), which can donate an electron to neutralize free radicals and ROS. When glutathione donates an electron, it becomes oxidized and forms glutathione disulfide (GSSG).

Glutathione disulfide is a dimer of two glutathione molecules linked by a disulfide bond (-S-S-) between the sulfur atoms of their cysteine residues. The body can recycle GSSG back to its reduced form (GSH) through the action of an enzyme called glutathione reductase, which requires NADPH as a reducing agent.

Maintaining a proper balance between GSH and GSSG is essential for cellular health, as it helps regulate various physiological processes such as DNA synthesis, gene expression, immune function, and apoptosis (programmed cell death). An imbalance in glutathione homeostasis can lead to oxidative stress, inflammation, and the development of various diseases.

Transferases are a class of enzymes that facilitate the transfer of specific functional groups (like methyl, acetyl, or phosphate groups) from one molecule (the donor) to another (the acceptor). This transfer of a chemical group can alter the physical or chemical properties of the acceptor molecule and is a crucial process in various metabolic pathways. Transferases play essential roles in numerous biological processes, such as biosynthesis, detoxification, and catabolism.

The classification of transferases is based on the type of functional group they transfer:

1. Methyltransferases - transfer a methyl group (-CH3)
2. Acetyltransferases - transfer an acetyl group (-COCH3)
3. Aminotransferases or Transaminases - transfer an amino group (-NH2 or -NHR, where R is a hydrogen atom or a carbon-containing group)
4. Glycosyltransferases - transfer a sugar moiety (a glycosyl group)
5. Phosphotransferases - transfer a phosphate group (-PO3H2)
6. Sulfotransferases - transfer a sulfo group (-SO3H)
7. Acyltransferases - transfer an acyl group (a fatty acid or similar molecule)

These enzymes are identified and named according to the systematic nomenclature of enzymes developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The naming convention includes the class of enzyme, the specific group being transferred, and the molecules involved in the transfer reaction. For example, the enzyme that transfers a phosphate group from ATP to glucose is named "glucokinase."

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

'Bufo bufo' is the scientific name for a species of toad commonly known as the common toad or European toad. It belongs to the family Bufonidae and is native to many parts of Europe and western Asia. The toad is typically characterized by its warty skin, large parotoid glands behind its eyes, and a dull yellow or brownish color.

The parotoid glands of Bufo bufo contain a toxic secretion that can be harmful if ingested or comes into contact with mucous membranes, making the toad unpalatable to many predators. The toxin can cause irritation and may lead to respiratory and cardiac problems in some animals, including pets and humans.

While Bufo bufo is not typically aggressive, it will defend itself if threatened by inflating its body, lifting its hind legs, and releasing the toxic secretion from its glands. The common toad is primarily a terrestrial animal but requires access to water for breeding, and it feeds on a variety of small invertebrates such as insects, worms, and slugs.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Metabolic detoxification, in the context of drugs, refers to the series of biochemical processes that the body undergoes to transform drugs or other xenobiotics into water-soluble compounds so they can be excreted. This process typically involves two phases:

1. Phase I Detoxification: In this phase, enzymes such as cytochrome P450 oxidases introduce functional groups into the drug molecule, making it more polar and reactive. This can result in the formation of metabolites that are less active than the parent compound or, in some cases, more toxic.

2. Phase II Detoxification: In this phase, enzymes such as glutathione S-transferases, UDP-glucuronosyltransferases, and sulfotransferases conjugate these polar and reactive metabolites with endogenous molecules like glutathione, glucuronic acid, or sulfate. This further increases the water solubility of the compound, allowing it to be excreted by the kidneys or bile.

It's important to note that while these processes are essential for eliminating drugs and other harmful substances from the body, they can also produce reactive metabolites that may cause damage to cells and tissues if not properly regulated. Therefore, maintaining a balance in the activity of these detoxification enzymes is crucial for overall health and well-being.

Octopodiformes is a taxonomic order that includes two main groups: octopuses (Octopoda) and vampire squids (Vampyroteuthis infernalis). This grouping is based on similarities in their fossil record and molecular data. Although they are commonly referred to as squids, vampire squids are not true squids, which belong to a different order called Teuthida.

Octopodiformes are characterized by several features, including:

1. A highly developed brain and complex nervous system.
2. Eight arms with suckers, but no tentacles.
3. The ability to change their skin color and texture for camouflage.
4. Three hearts that pump blood through their bodies.
5. Blue blood due to the copper-based protein hemocyanin.
6. A siphon used for jet propulsion and other functions, such as waste expulsion and mating.
7. Ink sacs for defense against predators.

Octopuses are known for their intelligence, problem-solving abilities, and short lifespans (usually less than two years). Vampire squids, on the other hand, live in deep ocean environments and have a unique feeding strategy that involves filtering organic matter from the water. They can also produce bioluminescent displays to confuse predators.

It is important to note that while Octopodiformes is a well-supported taxonomic group, there is still ongoing research and debate about the relationships among cephalopods (the class that includes octopuses, squids, cuttlefish, and nautiluses) and their classification.

Dichloroacetic acid (DCA) is a chemical compound with the formula CCl2CO2H. It is a colorless liquid that is used as a reagent in organic synthesis and as a laboratory research tool. DCA is also a byproduct of water chlorination and has been found to occur in low levels in some chlorinated drinking waters.

In the medical field, DCA has been studied for its potential anticancer effects. Preclinical studies have suggested that DCA may be able to selectively kill cancer cells by inhibiting the activity of certain enzymes involved in cell metabolism. However, more research is needed to determine whether DCA is safe and effective as a cancer treatment in humans.

It is important to note that DCA is not currently approved by regulatory agencies such as the U.S. Food and Drug Administration (FDA) for use as a cancer treatment. It should only be used in clinical trials or under the supervision of a qualified healthcare professional.

Butylated hydroxyanisole (BHA) is a synthetic antioxidant that is commonly used as a food additive to prevent or slow down the oxidation of fats, oils, and other lipids. This helps to maintain the quality, stability, and safety of food products by preventing rancidity and off-flavors. BHA is also used in cosmetics, pharmaceuticals, and animal feeds for similar purposes.

In medical terms, BHA is classified as a chemical preservative and antioxidant. It is a white or creamy white crystalline powder that is soluble in alcohol and ether but insoluble in water. BHA is often used in combination with other antioxidants, such as butylated hydroxytoluene (BHT), to provide a synergistic effect and enhance the overall stability of food products.

While BHA is generally recognized as safe by regulatory agencies such as the U.S. Food and Drug Administration (FDA) and the European Food Safety Authority (EFSA), some studies have suggested that high doses of BHA may have potential health risks, including possible carcinogenic effects. However, these findings are not conclusive, and further research is needed to fully understand the potential health impacts of BHA exposure.

Alkyl and aryl transferases are a group of enzymes that catalyze the transfer of alkyl or aryl groups from one molecule to another. These enzymes play a role in various biological processes, including the metabolism of drugs and other xenobiotics, as well as the biosynthesis of certain natural compounds.

Alkyl transferases typically catalyze the transfer of methyl or ethyl groups, while aryl transferases transfer larger aromatic rings. These enzymes often use cofactors such as S-adenosylmethionine (SAM) or acetyl-CoA to donate the alkyl or aryl group to a recipient molecule.

Examples of alkyl and aryl transferases include:

1. Methyltransferases: enzymes that transfer methyl groups from SAM to various acceptor molecules, such as DNA, RNA, proteins, and small molecules.
2. Histone methyltransferases: enzymes that methylate specific residues on histone proteins, which can affect chromatin structure and gene expression.
3. N-acyltransferases: enzymes that transfer acetyl or other acyl groups to amino groups in proteins or small molecules.
4. O-acyltransferases: enzymes that transfer acyl groups to hydroxyl groups in lipids, steroids, and other molecules.
5. Arylsulfatases: enzymes that remove sulfate groups from aromatic rings, releasing an alcohol and sulfate.
6. Glutathione S-transferases (GSTs): enzymes that transfer the tripeptide glutathione to electrophilic centers in xenobiotics and endogenous compounds, facilitating their detoxification and excretion.

Glutathione synthase is a type of enzyme involved in the synthesis of glutathione, a vital antioxidant that helps protect cells from damage caused by free radicals and peroxides. Glutathione synthase specifically catalyzes the final step in glutathione biosynthesis, which is the reaction between gamma-glutamylcysteine and glycine to form glutathione. This enzyme plays a crucial role in maintaining cellular health and function by helping to regulate oxidative stress and other important physiological processes.

"Maleate" is not a medical term in and of itself, but it is a chemical compound that can be found in some medications. Maleic acid or its salts (maleates) are used as a keratolytic agent in topical medications, which means they help to break down and remove dead skin cells. They can also be used as a preservative or a buffering agent in various pharmaceutical preparations.

Maleic acid is a type of organic compound known as a dicarboxylic acid, which contains two carboxyl groups. In the case of maleic acid, these carboxyl groups are located on a single carbon atom, which makes it a cis-conjugated diacid. This structural feature gives maleic acid unique chemical properties that can be useful in various pharmaceutical and industrial applications.

It's worth noting that maleic acid and its salts should not be confused with "maleate" as a gender-specific term, which refers to something related to or characteristic of males.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

Ethacrynic acid is a loop diuretic drug that is primarily used to treat edema (swelling) associated with heart failure, liver cirrhosis, and kidney disease. It works by increasing the excretion of water and sodium in the urine, which helps reduce fluid buildup in the body. Ethacrynic acid is also known as a "high-ceiling" diuretic because it has a strong effect on urine production.

The drug is available in oral form and is typically taken once or twice a day, depending on the severity of the edema and the patient's response to treatment. Ethacrynic acid can have side effects, including hearing loss, kidney damage, and electrolyte imbalances, so it is important for patients to be monitored closely by their healthcare provider while taking this medication.

It is worth noting that ethacrynic acid is not as commonly used as other loop diuretics, such as furosemide or torsemide, due to its higher risk of side effects and the availability of safer alternatives.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Proteus mirabilis is a species of Gram-negative, facultatively anaerobic, rod-shaped bacteria that are commonly found in the environment, particularly in soil and water. In humans, P. mirabilis can be part of the normal gut flora but can also cause opportunistic infections, particularly in the urinary tract. It is known for its ability to produce urease, which can lead to the formation of urinary stones and blockages.

P. mirabilis infections are often associated with underlying medical conditions such as diabetes, kidney disease, or urinary catheterization. Symptoms of a P. mirabilis infection may include fever, cloudy or foul-smelling urine, and pain or burning during urination. Treatment typically involves antibiotics that are effective against Gram-negative bacteria, although resistance to certain antibiotics is not uncommon in P. mirabilis isolates.

Alkenes are unsaturated hydrocarbons that contain at least one carbon-carbon double bond in their molecular structure. The general chemical formula for alkenes is CnH2n, where n represents the number of carbon atoms in the molecule.

The double bond in alkenes can undergo various reactions, such as addition reactions, where different types of molecules can add across the double bond to form new compounds. The relative position of the double bond in the carbon chain and the presence of substituents on the carbon atoms can affect the physical and chemical properties of alkenes.

Alkenes are important industrial chemicals and are used as starting materials for the synthesis of a wide range of products, including plastics, resins, fibers, and other chemicals. They are also found in nature, occurring in some plants and animals, and can be produced by certain types of bacteria through fermentation processes.

S-Nitrosoglutathione (GSNO) is defined as a type of nitrosothiol, which is a class of compounds containing a nitroso (−NO) group attached to a sulfur atom. Specifically, GSNO is the result of the attachment of a nitric oxide (NO) molecule to the sulfur atom of the tripeptide glutathione (GSH). This compound has been the subject of extensive research due to its potential role in the regulation of various biological processes, including cell signaling, vasodilation, and neurotransmission, among others. It is also known to have antioxidant properties and to play a role in the immune response. However, it should be noted that abnormal levels of GSNO have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and cardiovascular disorders.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

Oxidative stress is defined as an imbalance between the production of reactive oxygen species (free radicals) and the body's ability to detoxify them or repair the damage they cause. This imbalance can lead to cellular damage, oxidation of proteins, lipids, and DNA, disruption of cellular functions, and activation of inflammatory responses. Prolonged or excessive oxidative stress has been linked to various health conditions, including cancer, cardiovascular diseases, neurodegenerative disorders, and aging-related diseases.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

Buthionine Sulfoximine (BSO) is a chemical compound that is known to inhibit the enzyme gamma-glutamylcysteine synthetase, which plays a crucial role in the production of glutathione, a powerful antioxidant in the body. By inhibiting this enzyme, BSO can deplete glutathione levels in cells, making it a useful tool in research to study the effects of glutathione depletion on various biological processes. It is often used in laboratory experiments and clinical trials for its potential therapeutic benefits in cancer treatment and other diseases associated with oxidative stress. However, its use as a therapeutic agent is still being investigated and has not yet been approved by regulatory agencies for widespread clinical use.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Isothiocyanates are organic compounds that contain a functional group made up of a carbon atom, a nitrogen atom, and a sulfur atom, with the formula RN=C=S (where R can be an alkyl or aryl group). They are commonly found in cruciferous vegetables such as broccoli, brussels sprouts, and wasabi. Isothiocyanates have been studied for their potential health benefits, including their anticancer and anti-inflammatory properties. However, they can also be toxic in high concentrations.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Amitrole is a non-selective herbicide that is used to control broadleaf weeds and some annual grasses. Its chemical name is 3-amino-1,2,4-triazole, and it works by inhibiting the enzyme responsible for the production of certain aromatic amino acids in plants, which are essential for their growth and development.

Amitrole is absorbed through the leaves and roots of plants and can be applied either before or after weed emergence. It is commonly used in agricultural settings, as well as in non-crop areas such as industrial sites, railways, and roadsides.

While amitrole is generally considered safe for use around humans and animals when used according to label instructions, it can cause eye and skin irritation, and may be harmful if swallowed or inhaled. It is important to follow all safety precautions when handling and applying this herbicide.

Aldehydes are a class of organic compounds characterized by the presence of a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bonded oxygen atom, also known as a formyl or aldehyde group. The general chemical structure of an aldehyde is R-CHO, where R represents a hydrocarbon chain.

Aldehydes are important in biochemistry and medicine as they are involved in various metabolic processes and are found in many biological molecules. For example, glucose is converted to pyruvate through a series of reactions that involve aldehyde intermediates. Additionally, some aldehydes have been identified as toxicants or environmental pollutants, such as formaldehyde, which is a known carcinogen and respiratory irritant.

Formaldehyde is also commonly used in medical and laboratory settings for its disinfectant properties and as a fixative for tissue samples. However, exposure to high levels of formaldehyde can be harmful to human health, causing symptoms such as coughing, wheezing, and irritation of the eyes, nose, and throat. Therefore, appropriate safety measures must be taken when handling aldehydes in medical and laboratory settings.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Quinone reductases are a group of enzymes that catalyze the reduction of quinones to hydroquinones, using NADH or NADPH as an electron donor. This reaction is important in the detoxification of quinones, which are potentially toxic compounds produced during the metabolism of certain drugs, chemicals, and endogenous substances.

There are two main types of quinone reductases: NQO1 (NAD(P)H:quinone oxidoreductase 1) and NQO2 (NAD(P)H:quinone oxidoreductase 2). NQO1 is a cytosolic enzyme that can reduce a wide range of quinones, while NQO2 is a mitochondrial enzyme with a narrower substrate specificity.

Quinone reductases have been studied for their potential role in cancer prevention and treatment, as they may help to protect cells from oxidative stress and DNA damage caused by quinones and other toxic compounds. Additionally, some quinone reductase inhibitors have been developed as chemotherapeutic agents, as they can enhance the cytotoxicity of certain drugs that require quinone reduction for activation.

Antioxidants are substances that can prevent or slow damage to cells caused by free radicals, which are unstable molecules that the body produces as a reaction to environmental and other pressures. Antioxidants are able to neutralize free radicals by donating an electron to them, thus stabilizing them and preventing them from causing further damage to the cells.

Antioxidants can be found in a variety of foods, including fruits, vegetables, nuts, and grains. Some common antioxidants include vitamins C and E, beta-carotene, and selenium. Antioxidants are also available as dietary supplements.

In addition to their role in protecting cells from damage, antioxidants have been studied for their potential to prevent or treat a number of health conditions, including cancer, heart disease, and age-related macular degeneration. However, more research is needed to fully understand the potential benefits and risks of using antioxidant supplements.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

"Inbred strains of rats" are genetically identical rodents that have been produced through many generations of brother-sister mating. This results in a high degree of homozygosity, where the genes at any particular locus in the genome are identical in all members of the strain.

Inbred strains of rats are widely used in biomedical research because they provide a consistent and reproducible genetic background for studying various biological phenomena, including the effects of drugs, environmental factors, and genetic mutations on health and disease. Additionally, inbred strains can be used to create genetically modified models of human diseases by introducing specific mutations into their genomes.

Some commonly used inbred strains of rats include the Wistar Kyoto (WKY), Sprague-Dawley (SD), and Fischer 344 (F344) rat strains. Each strain has its own unique genetic characteristics, making them suitable for different types of research.

Triethyltin compounds refer to organotin substances that contain the triethyltin (C2H5)3Sn- group. These compounds have been used in various industrial applications, such as biocides and polyvinyl chloride stabilizers. However, they are highly toxic and can cause neurological damage in humans and animals. Long-term exposure to triethyltin compounds has been linked to symptoms including headaches, memory loss, tremors, and seizures.

Steroid isomerases are a class of enzymes that catalyze the interconversion of steroids by rearranging various chemical bonds within their structures, leading to the formation of isomers. These enzymes play crucial roles in steroid biosynthesis and metabolism, enabling the production of a diverse array of steroid hormones with distinct biological activities.

There are several types of steroid isomerases, including:

1. 3-beta-hydroxysteroid dehydrogenase/delta(5)-delta(4) isomerase (3-beta-HSD): This enzyme catalyzes the conversion of delta(5) steroids to delta(4) steroids, accompanied by the oxidation of a 3-beta-hydroxyl group to a keto group. It is essential for the biosynthesis of progesterone, cortisol, and aldosterone.
2. Aromatase: This enzyme converts androgens (such as testosterone) into estrogens (such as estradiol) by introducing a phenolic ring, which results in the formation of an aromatic A-ring. It is critical for the development and maintenance of female secondary sexual characteristics.
3. 17-beta-hydroxysteroid dehydrogenase (17-beta-HSD): This enzyme catalyzes the interconversion between 17-keto and 17-beta-hydroxy steroids, playing a key role in the biosynthesis of estrogens, androgens, and glucocorticoids.
4. 5-alpha-reductase: This enzyme catalyzes the conversion of testosterone to dihydrotestosterone (DHT) by reducing the double bond between carbons 4 and 5 in the A-ring. DHT is a more potent androgen than testosterone, playing essential roles in male sexual development and prostate growth.
5. 20-alpha-hydroxysteroid dehydrogenase (20-alpha-HSD): This enzyme catalyzes the conversion of corticosterone to aldosterone, a critical mineralocorticoid involved in regulating electrolyte and fluid balance.
6. 3-beta-hydroxysteroid dehydrogenase (3-beta-HSD): This enzyme catalyzes the conversion of pregnenolone to progesterone and 17-alpha-hydroxypregnenolone to 17-alpha-hydroxyprogesterone, which are essential intermediates in steroid hormone biosynthesis.

These enzymes play crucial roles in the biosynthesis, metabolism, and elimination of various steroid hormones, ensuring proper endocrine function and homeostasis. Dysregulation or mutations in these enzymes can lead to various endocrine disorders, including congenital adrenal hyperplasia (CAH), polycystic ovary syndrome (PCOS), androgen insensitivity syndrome (AIS), and others.

Butanones are a group of chemical compounds that contain a ketone functional group and have the molecular formula C4H8O. They are also known as methyl ethyl ketones or MEKs. The simplest butanone is called methyl ethyl ketone (MEK) or 2-butanone, which has a chain of four carbon atoms with a ketone group in the second position. Other butanones include diethyl ketone (3-pentanone), which has a ketone group in the third position, and methyl isobutyl ketone (MIBK) or 4-methyl-2-pentanone, which has a branched chain with a ketone group in the second position.

Butanones are commonly used as solvents in various industrial applications, such as paint thinners, adhesives, and cleaning agents. They have a characteristic odor and can be harmful if ingested or inhaled in large quantities. Exposure to butanones can cause irritation of the eyes, skin, and respiratory tract, and prolonged exposure may lead to neurological symptoms such as dizziness, headache, and nausea.

Methylene chloride, also known as dichloromethane, is an organic compound with the formula CH2Cl2. It is a colorless, volatile liquid with a mild sweet aroma. In terms of medical definitions, methylene chloride is not typically included due to its primarily industrial uses. However, it is important to note that exposure to high levels of methylene chloride can cause harmful health effects, including irritation to the eyes, skin, and respiratory tract; headaches; dizziness; and, at very high concentrations, unconsciousness and death. Chronic exposure to methylene chloride has been linked to liver toxicity, and it is considered a possible human carcinogen by the International Agency for Research on Cancer (IARC).

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

I'd be happy to help! However, it seems there might be a slight confusion in your question. Hydrocarbons and iodinated compounds are two different types of chemical substances.

Hydrocarbons refer to organic compounds consisting entirely of hydrogen and carbon atoms. They can be categorized into several types, such as alkanes, alkenes, alkynes, and aromatic hydrocarbons, based on their structure and properties.

On the other hand, iodinated compounds are organic or inorganic molecules containing iodine atoms. These compounds have various applications, especially in medical imaging and therapy, such as radioactive iodine therapy for thyroid cancer and the use of iodinated contrast agents in X-ray and CT scans.

There isn't a specific category called "iodinated hydrocarbons" since hydrocarbons don't inherently contain iodine. However, it is possible to create molecules that combine both hydrocarbon structures and iodine atoms. An example of such a compound would be iodinated alkanes, where iodine atoms replace some hydrogen atoms in an alkane molecule.

So, if you're looking for a medical definition related to iodinated compounds, I can provide that. If you meant something else, please let me know!

Lipid peroxides are chemical compounds that form when lipids (fats or fat-like substances) oxidize. This process, known as lipid peroxidation, involves the reaction of lipids with oxygen in a way that leads to the formation of hydroperoxides and various aldehydes, such as malondialdehyde.

Lipid peroxidation is a naturally occurring process that can also be accelerated by factors such as exposure to radiation, certain chemicals, or enzymatic reactions. It plays a role in many biological processes, including cell signaling and regulation of gene expression, but it can also contribute to the development of various diseases when it becomes excessive.

Examples of lipid peroxides include phospholipid hydroperoxides, cholesteryl ester hydroperoxides, and triglyceride hydroperoxides. These compounds are often used as markers of oxidative stress in biological systems and have been implicated in the pathogenesis of atherosclerosis, cancer, neurodegenerative diseases, and other conditions associated with oxidative damage.

Trialkyltin compounds are a category of organotin (oceanic) chemicals, characterized by the presence of three alkyl groups bonded to a tin atom. The general formula for these compounds is (CnH2n+1)3Sn, where n represents the number of carbon atoms in each alkyl group.

These compounds have been used in various industrial applications such as biocides, heat stabilizers, and PVC plasticizers. However, due to their high toxicity, environmental persistence, and potential bioaccumulation, their use has been restricted or banned in many countries.

Examples of trialkyltin compounds include tributyltin (TBT) and triphenyltin (TPT). TBT was widely used as an antifouling agent in marine paints to prevent the growth of barnacles, algae, and other organisms on ship hulls. However, due to its detrimental effects on marine life, particularly on shellfish and mollusks, its use has been largely phased out.

Trialkyltin compounds can have toxic effects on both aquatic and terrestrial organisms, including humans. They can cause neurological damage, impaired immune function, reproductive issues, and developmental abnormalities in various species.

Lipid peroxidation is a process in which free radicals, such as reactive oxygen species (ROS), steal electrons from lipids containing carbon-carbon double bonds, particularly polyunsaturated fatty acids (PUFAs). This results in the formation of lipid hydroperoxides, which can decompose to form a variety of compounds including reactive carbonyl compounds, aldehydes, and ketones.

Malondialdehyde (MDA) is one such compound that is commonly used as a marker for lipid peroxidation. Lipid peroxidation can cause damage to cell membranes, leading to changes in their fluidity and permeability, and can also result in the modification of proteins and DNA, contributing to cellular dysfunction and ultimately cell death. It is associated with various pathological conditions such as atherosclerosis, neurodegenerative diseases, and cancer.

Nitrobenzenes are organic compounds that contain a nitro group (-NO2) attached to a benzene ring. The chemical formula for nitrobenzene is C6H5NO2. It is a pale yellow, oily liquid with a characteristic sweet and unpleasant odor. Nitrobenzene is not produced or used in large quantities in the United States, but it is still used as an intermediate in the production of certain chemicals.

Nitrobenzenes are classified as toxic and harmful if swallowed, inhaled, or if they come into contact with the skin. They can cause irritation to the eyes, skin, and respiratory tract, and prolonged exposure can lead to more serious health effects such as damage to the nervous system and liver. Nitrobenzenes are also considered to be potential carcinogens, meaning that they may increase the risk of cancer with long-term exposure.

In a medical setting, nitrobenzene poisoning is rare but can occur if someone is exposed to large amounts of this chemical. Symptoms of nitrobenzene poisoning may include headache, dizziness, nausea, vomiting, and difficulty breathing. In severe cases, it can cause convulsions, unconsciousness, and even death. If you suspect that you or someone else has been exposed to nitrobenzenes, it is important to seek medical attention immediately.

Phenylglyoxal is not typically considered a medical term, but it does have relevance to the field of biochemistry and medicine. Here's a definition:

Phenylglyoxal (also known as pyruvic aldehyde or 2-oxophenyle) is an organic compound with the formula C6H5CHO. It is a white crystalline solid that is soluble in water and polar organic solvents. Phenylglyoxal is used primarily for research purposes, particularly in the study of glycation and protein modifications.

In biochemistry, phenylglyoxal is known as a glycating agent, which means it can react with amino groups in proteins to form advanced glycation end-products (AGEs). This reaction can alter the structure and function of proteins, contributing to aging and various diseases such as diabetes, neurodegenerative disorders, and cardiovascular disease.

While phenylglyoxal itself is not a medical term, its role in protein modification and glycation has implications for understanding the pathophysiology of several medical conditions.

Anisoles are organic compounds that consist of a phenyl ring (a benzene ring with a hydroxyl group replaced by a hydrogen atom) attached to a methoxy group (-O-CH3). The molecular formula for anisole is C6H5OCH3. Anisoles are aromatic ethers and can be found in various natural sources, including anise plants and some essential oils. They have a wide range of applications, including as solvents, flavoring agents, and intermediates in the synthesis of other chemicals.

Lactoylglutathione lyase is not a commonly used term in medicine, but it is a biochemical term that refers to an enzyme also known as glyoxalase I. This enzyme plays a role in the detoxification of methylglyoxal, a reactive dicarbonyl compound that can cause damage to proteins and DNA. Methylglyoxal is produced during normal metabolic processes, particularly in the breakdown of glucose and other sugars.

Glyoxalase I catalyzes the conversion of hemithioacetal (formed from methylglyoxal and glutathione) to S-D-lactoylglutathione, which is then converted to D-lactic acid and glutathione by glyoxalase II. The overall reaction helps to prevent the accumulation of toxic levels of methylglyoxal in cells.

Defects or mutations in the gene that encodes for glyoxalase I can lead to an increased risk of developing certain diseases, such as diabetes and neurodegenerative disorders.

DNA nucleotidylexotransferase is not a widely recognized or established medical term. It appears to be a combination of the terms "DNA," "nucleotide," and "lexotransferase," but the specific meaning or function of this enzyme is unclear.

"DNA" refers to deoxyribonucleic acid, which is the genetic material found in the cells of most living organisms.

"Nucleotide" refers to a molecule that consists of a nitrogenous base, a sugar, and one or more phosphate groups. Nucleotides are the building blocks of DNA and RNA.

"Lexotransferase" is not a recognized enzyme class or function. It may be a typographical error or a term that has been misused or misunderstood.

Therefore, it is not possible to provide a medical definition for 'DNA nucleotidylexotransferase'. If you have more information about the context in which this term was used, I may be able to provide further clarification.

I'm sorry for any confusion, but "Ditiocarb" is not a recognized medical term or abbreviation in standard medical or clinical contexts. It's possible that you may have made a typo or are referring to a term from a different field. If you have more information or if there's a specific context in which you encountered this term, I'd be happy to help further!

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

Glutamate-cysteine ligase (GCL) is an essential enzyme in the biosynthesis of glutathione, a major antioxidant in cells. It catalyzes the reaction between glutamate and cysteine to form γ-glutamylcysteine, which is then combined with glycine by glutathione synthetase to produce glutathione.

GCL has two subunits: a catalytic subunit (GCLC) and a modulatory subunit (GCLM). The former contains the active site for the formation of the peptide bond between glutamate and cysteine, while the latter regulates the activity of GCLC by affecting its sensitivity to feedback inhibition by glutathione.

The proper functioning of GCL is critical for maintaining cellular redox homeostasis and protecting against oxidative stress, making it a potential target for therapeutic intervention in various diseases associated with oxidative damage, such as neurodegenerative disorders, cancer, and aging-related conditions.

I apologize for any confusion, but "Sulfinic Acids" is not a term used in medical definitions. It is a term from the field of chemistry. Sulfinic acids are organic compounds that contain a functional group with the formula RSO(O)H, where R represents an alkyl or aryl group. They are important intermediates in organic synthesis and can be found in some natural sources. If you have any questions related to medical terminology or concepts, I would be happy to help!

Coenzyme A-transferases are a group of enzymes that catalyze the transfer of Coenzyme A (CoA) from one molecule to another. CoA is a coenzyme that plays a crucial role in various metabolic processes, including the oxidation of carbohydrates, fatty acids, and amino acids.

Coenzyme A-transferases can be further classified into several subfamilies based on their specific functions and the types of molecules they act upon. For example, some CoA-transferases transfer CoA to acyl groups, forming acyl-CoAs, which are important intermediates in fatty acid metabolism. Other CoA-transferases transfer CoA to pyruvate, forming pyruvate dehydrogenase complexes that play a key role in glucose metabolism.

These enzymes are essential for maintaining the proper functioning of various metabolic pathways and are involved in a wide range of physiological processes, including energy production, lipid synthesis, and detoxification. Defects in CoA-transferases can lead to several metabolic disorders, such as fatty acid oxidation disorders and pyruvate dehydrogenase deficiency.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Experimental liver neoplasms refer to abnormal growths or tumors in the liver that are intentionally created or manipulated in a laboratory setting for the purpose of studying their development, progression, and potential treatment options. These experimental models can be established using various methods such as chemical induction, genetic modification, or transplantation of cancerous cells or tissues. The goal of this research is to advance our understanding of liver cancer biology and develop novel therapies for liver neoplasms in humans. It's important to note that these experiments are conducted under strict ethical guidelines and regulations to minimize harm and ensure the humane treatment of animals involved in such studies.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Leukotriene A4 (LTA4) is a lipid mediator derived from arachidonic acid, which is released from membrane phospholipids by the action of phospholipase A2. LTA4 is synthesized in the cell through the 5-lipoxygenase pathway and serves as an intermediate in the production of other leukotrienes (LB4, LTC4, LTD4, LTE4) that are involved in inflammation, bronchoconstriction, increased vascular permeability, and recruitment of leukocytes.

Leukotriene A4 is an unstable compound with a short half-life, which can be converted to Leukotriene B4 (LTB4) by the enzyme LTA4 hydrolase or to Leukotriene C4 (LTC4) by the addition of glutathione through the action of LTC4 synthase. These leukotrienes play a significant role in the pathophysiology of asthma, allergies, and other inflammatory diseases.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Catalase is a type of enzyme that is found in many living organisms, including humans. Its primary function is to catalyze the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from the harmful effects of hydrogen peroxide, which can be toxic at high concentrations.

The chemical reaction catalyzed by catalase can be represented as follows:

H2O2 + Catalase → H2O + O2 + Catalase

Catalase is a powerful antioxidant enzyme that plays an important role in protecting cells from oxidative damage. It is found in high concentrations in tissues that produce or are exposed to hydrogen peroxide, such as the liver, kidneys, and erythrocytes (red blood cells).

Deficiency in catalase activity has been linked to several diseases, including cancer, neurodegenerative disorders, and aging. On the other hand, overexpression of catalase has been shown to have potential therapeutic benefits in various disease models, such as reducing inflammation and oxidative stress.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Sulfobromophthalein (BSP or bromsulphthalein) is not typically defined in a medical dictionary as it is a chemical compound. However, I can provide you with some information about its use in a medical context:

Sulfobromophthalein is a chemical compound primarily used for liver function tests. It is a dye that is injected into the patient's bloodstream, and then its clearance rate from the blood is measured to evaluate liver function. A healthy liver should quickly remove the dye from the blood and excrete it through the bile ducts into the digestive system. If the liver is not functioning properly, the clearance of sulfobromophthalein will be slower, leading to higher levels of the dye remaining in the bloodstream over time.

The test using sulfobromophthalein has largely been replaced by more modern and specific liver function tests; however, it was once widely used for assessing overall liver health and diagnosing conditions such as hepatitis, cirrhosis, and liver damage due to various causes.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Isoelectric focusing (IEF) is a technique used in electrophoresis, which is a method for separating proteins or other molecules based on their electrical charges. In IEF, a mixture of ampholytes (molecules that can carry both positive and negative charges) is used to create a pH gradient within a gel matrix. When an electric field is applied, the proteins or molecules migrate through the gel until they reach the point in the gradient where their net charge is zero, known as their isoelectric point (pI). At this point, they focus into a sharp band and stop moving, resulting in a highly resolved separation of the different components based on their pI. This technique is widely used in protein research for applications such as protein identification, characterization, and purification.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Indolequinones are a type of chemical compound that consist of an indole ring, which is a heterocyclic aromatic organic compound, fused to a quinone ring. They can be found in some natural sources, including certain types of bacteria and fungi, as well as in synthetic forms.

Indolequinones have been studied for their potential use in medical treatments, particularly in the area of cancer research. Some indolequinones have been shown to have antitumor properties and are being investigated as possible chemotherapeutic agents. However, they can also be toxic and may have side effects, so further research is needed to determine their safety and effectiveness for medical use.

Adrenochrome is a chemical compound that is formed when adrenaline (epinephrine) is oxidized. It is not a naturally occurring hormone or neurotransmitter, but rather a byproduct of the breakdown of these substances. The existence of adrenochrome in the human body is controversial and its effects on the human brain are not well understood.

In popular culture, adrenochrome has been associated with theories about its psychoactive properties and alleged use as a drug in illegal or illicit activities. However, there is no scientific evidence to support these claims and they should be regarded with skepticism. The misinformation surrounding adrenochrome may have originated from Hunter S. Thompson's book "Fear and Loathing in Las Vegas," where it was described as a drug that produces intense hallucinations and feelings of euphoria. However, this portrayal is not based on any scientific evidence and should be considered fiction.

Xenobiotics are substances that are foreign to a living organism and usually originate outside of the body. This term is often used in the context of pharmacology and toxicology to refer to drugs, chemicals, or other agents that are not naturally produced by or expected to be found within the body.

When xenobiotics enter the body, they undergo a series of biotransformation processes, which involve metabolic reactions that convert them into forms that can be more easily excreted from the body. These processes are primarily carried out by enzymes in the liver and other organs.

It's worth noting that some xenobiotics can have beneficial effects on the body when used as medications or therapeutic agents, while others can be harmful or toxic. Therefore, understanding how the body metabolizes and eliminates xenobiotics is important for developing safe and effective drugs, as well as for assessing the potential health risks associated with exposure to environmental chemicals and pollutants.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Gamma-glutamyltransferase (GGT), also known as gamma-glutamyl transpeptidase, is an enzyme found in many tissues, including the liver, bile ducts, and pancreas. GGT is involved in the metabolism of certain amino acids and plays a role in the detoxification of various substances in the body.

GGT is often measured as a part of a panel of tests used to evaluate liver function. Elevated levels of GGT in the blood may indicate liver disease or injury, bile duct obstruction, or alcohol consumption. However, it's important to note that several other factors can also affect GGT levels, so abnormal results should be interpreted in conjunction with other clinical findings and diagnostic tests.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Phenobarbital is a barbiturate medication that is primarily used for the treatment of seizures and convulsions. It works by suppressing the abnormal electrical activity in the brain that leads to seizures. In addition to its anticonvulsant properties, phenobarbital also has sedative and hypnotic effects, which can be useful for treating anxiety, insomnia, and agitation.

Phenobarbital is available in various forms, including tablets, capsules, and elixirs, and it is typically taken orally. The medication works by binding to specific receptors in the brain called gamma-aminobutyric acid (GABA) receptors, which help to regulate nerve impulses in the brain. By increasing the activity of GABA, phenobarbital can help to reduce excessive neural activity and prevent seizures.

While phenobarbital is an effective medication for treating seizures and other conditions, it can also be habit-forming and carries a risk of dependence and addiction. Long-term use of the medication can lead to tolerance, meaning that higher doses may be needed to achieve the same effects. Abruptly stopping the medication can also lead to withdrawal symptoms, such as anxiety, restlessness, and seizures.

Like all medications, phenobarbital can have side effects, including dizziness, drowsiness, and impaired coordination. It can also interact with other medications, such as certain antidepressants and sedatives, so it is important to inform your healthcare provider of all medications you are taking before starting phenobarbital.

In summary, phenobarbital is a barbiturate medication used primarily for the treatment of seizures and convulsions. It works by binding to GABA receptors in the brain and increasing their activity, which helps to reduce excessive neural activity and prevent seizures. While phenobarbital can be effective, it carries a risk of dependence and addiction and can have side effects and drug interactions.

The isoelectric point (pI) is a term used in biochemistry and molecular biology to describe the pH at which a molecule, such as a protein or peptide, carries no net electrical charge. At this pH, the positive and negative charges on the molecule are equal and balanced. The pI of a protein can be calculated based on its amino acid sequence and is an important property that affects its behavior in various chemical and biological environments. Proteins with different pIs may have different solubilities, stabilities, and interactions with other molecules, which can impact their function and role in the body.

Medical Definition:

Superoxide dismutase (SOD) is an enzyme that catalyzes the dismutation of superoxide radicals (O2-) into oxygen (O2) and hydrogen peroxide (H2O2). This essential antioxidant defense mechanism helps protect the body's cells from damage caused by reactive oxygen species (ROS), which are produced during normal metabolic processes and can lead to oxidative stress when their levels become too high.

There are three main types of superoxide dismutase found in different cellular locations:
1. Copper-zinc superoxide dismutase (CuZnSOD or SOD1) - Present mainly in the cytoplasm of cells.
2. Manganese superoxide dismutase (MnSOD or SOD2) - Located within the mitochondrial matrix.
3. Extracellular superoxide dismutase (EcSOD or SOD3) - Found in the extracellular spaces, such as blood vessels and connective tissues.

Imbalances in SOD levels or activity have been linked to various pathological conditions, including neurodegenerative diseases, cancer, and aging-related disorders.

Methionine Sulfoximine (MSO) is not a medical term itself, but it is a compound that has been used in research and scientific studies. It's a stable analogue of the essential amino acid methionine, which can be found in some foods like sesame seeds, Brazil nuts, and fish.

Methionine Sulfoximine has been used in research to study the metabolism and transport of methionine in cells and organisms. It is also known for its ability to inhibit the enzyme cystathionine β-synthase (CBS), which plays a role in the metabolism of homocysteine, an amino acid associated with cardiovascular disease when present at high levels.

However, Methionine Sulfoximine is not used as a therapeutic agent or medication in humans due to its potential toxicity and lack of established clinical benefits.

Stilbenes are a type of chemical compound that consists of a 1,2-diphenylethylene backbone. They are phenolic compounds and can be found in various plants, where they play a role in the defense against pathogens and stress conditions. Some stilbenes have been studied for their potential health benefits, including their antioxidant and anti-inflammatory effects. One well-known example of a stilbene is resveratrol, which is found in the skin of grapes and in red wine.

It's important to note that while some stilbenes have been shown to have potential health benefits in laboratory studies, more research is needed to determine their safety and effectiveness in humans. It's always a good idea to talk to a healthcare provider before starting any new supplement regimen.

Affinity chromatography is a type of chromatography technique used in biochemistry and molecular biology to separate and purify proteins based on their biological characteristics, such as their ability to bind specifically to certain ligands or molecules. This method utilizes a stationary phase that is coated with a specific ligand (e.g., an antibody, antigen, receptor, or enzyme) that selectively interacts with the target protein in a sample.

The process typically involves the following steps:

1. Preparation of the affinity chromatography column: The stationary phase, usually a solid matrix such as agarose beads or magnetic beads, is modified by covalently attaching the ligand to its surface.
2. Application of the sample: The protein mixture is applied to the top of the affinity chromatography column, allowing it to flow through the stationary phase under gravity or pressure.
3. Binding and washing: As the sample flows through the column, the target protein selectively binds to the ligand on the stationary phase, while other proteins and impurities pass through. The column is then washed with a suitable buffer to remove any unbound proteins and contaminants.
4. Elution of the bound protein: The target protein can be eluted from the column using various methods, such as changing the pH, ionic strength, or polarity of the buffer, or by introducing a competitive ligand that displaces the bound protein.
5. Collection and analysis: The eluted protein fraction is collected and analyzed for purity and identity, often through techniques like SDS-PAGE or mass spectrometry.

Affinity chromatography is a powerful tool in biochemistry and molecular biology due to its high selectivity and specificity, enabling the efficient isolation of target proteins from complex mixtures. However, it requires careful consideration of the binding affinity between the ligand and the protein, as well as optimization of the elution conditions to minimize potential damage or denaturation of the purified protein.

Thiocyanates are chemical compounds that contain the thiocyanate ion (SCN-), which consists of a sulfur atom, a carbon atom, and a nitrogen atom. The thiocyanate ion is formed by the removal of a hydrogen ion from thiocyanic acid (HSCN). Thiocyanates are used in various applications, including pharmaceuticals, agrochemicals, and industrial chemicals. In medicine, thiocyanates have been studied for their potential effects on the thyroid gland and their use as a treatment for cyanide poisoning. However, excessive exposure to thiocyanates can be harmful and may cause symptoms such as irritation of the eyes, skin, and respiratory tract, as well as potential impacts on thyroid function.

The placenta is an organ that develops in the uterus during pregnancy and provides oxygen and nutrients to the growing baby through the umbilical cord. It also removes waste products from the baby's blood. The placenta attaches to the wall of the uterus, and the baby's side of the placenta contains many tiny blood vessels that connect to the baby's circulatory system. This allows for the exchange of oxygen, nutrients, and waste between the mother's and baby's blood. After the baby is born, the placenta is usually expelled from the uterus in a process called afterbirth.

Immunodiffusion is a laboratory technique used in immunology to detect and measure the presence of specific antibodies or antigens in a sample. It is based on the principle of diffusion, where molecules move from an area of high concentration to an area of low concentration until they reach equilibrium. In this technique, a sample containing an unknown quantity of antigen or antibody is placed in a gel or agar medium that contains a known quantity of antibody or antigen, respectively.

The two substances then diffuse towards each other and form a visible precipitate at the point where they meet and reach equivalence, which indicates the presence and quantity of the specific antigen or antibody in the sample. There are several types of immunodiffusion techniques, including radial immunodiffusion (RID) and double immunodiffusion (Ouchterlony technique). These techniques are widely used in diagnostic laboratories to identify and measure various antigens and antibodies, such as those found in infectious diseases, autoimmune disorders, and allergic reactions.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Sulfhydryl reagents are chemical compounds that react with sulfhydryl groups (-SH), which are found in certain amino acids such as cysteine. These reagents can be used to modify or inhibit the function of proteins by forming disulfide bonds or adding functional groups to the sulfur atom. Examples of sulfhydryl reagents include N-ethylmaleimide (NEM), p-chloromercuribenzoate (PCMB), and iodoacetamide. These reagents are widely used in biochemistry and molecular biology research to study protein structure and function, as well as in the development of drugs and therapeutic agents.

Ethylmaleimide is a chemical compound that is commonly used in research and scientific studies. Its chemical formula is C7H10N2S. It is known to modify proteins by forming covalent bonds with them, which can alter their function or structure. This property makes it a useful tool in the study of protein function and interactions.

In a medical context, Ethylmaleimide is not used as a therapeutic agent due to its reactivity and potential toxicity. However, it has been used in research to investigate various physiological processes, including the regulation of ion channels and the modulation of enzyme activity. It is important to note that the use of Ethylmaleimide in medical research should be carried out with appropriate precautions and safety measures due to its potential hazards.

Hypophysectomy is a surgical procedure that involves the removal or partial removal of the pituitary gland, also known as the hypophysis. The pituitary gland is a small endocrine gland located at the base of the brain, just above the nasal cavity, and is responsible for producing and secreting several important hormones that regulate various bodily functions.

Hypophysectomy may be performed for therapeutic or diagnostic purposes. In some cases, it may be used to treat pituitary tumors or other conditions that affect the function of the pituitary gland. It may also be performed as a research procedure in animal models to study the effects of pituitary hormone deficiency on various physiological processes.

The surgical approach for hypophysectomy may vary depending on the specific indication and the patient's individual anatomy. In general, however, the procedure involves making an incision in the skull and exposing the pituitary gland through a small opening in the bone. The gland is then carefully dissected and removed or partially removed as necessary.

Potential complications of hypophysectomy include damage to surrounding structures such as the optic nerves, which can lead to vision loss, and cerebrospinal fluid leaks. Additionally, removal of the pituitary gland can result in hormonal imbalances that may require long-term management with hormone replacement therapy.

Disulfides are a type of organic compound that contains a sulfur-sulfur bond. In the context of biochemistry and medicine, disulfide bonds are often found in proteins, where they play a crucial role in maintaining their three-dimensional structure and function. These bonds form when two sulfhydryl groups (-SH) on cysteine residues within a protein molecule react with each other, releasing a molecule of water and creating a disulfide bond (-S-S-) between the two cysteines. Disulfide bonds can be reduced back to sulfhydryl groups by various reducing agents, which is an important process in many biological reactions. The formation and reduction of disulfide bonds are critical for the proper folding, stability, and activity of many proteins, including those involved in various physiological processes and diseases.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Drug resistance, also known as antimicrobial resistance, is the ability of a microorganism (such as bacteria, viruses, fungi, or parasites) to withstand the effects of a drug that was originally designed to inhibit or kill it. This occurs when the microorganism undergoes genetic changes that allow it to survive in the presence of the drug. As a result, the drug becomes less effective or even completely ineffective at treating infections caused by these resistant organisms.

Drug resistance can develop through various mechanisms, including mutations in the genes responsible for producing the target protein of the drug, alteration of the drug's target site, modification or destruction of the drug by enzymes produced by the microorganism, and active efflux of the drug from the cell.

The emergence and spread of drug-resistant microorganisms pose significant challenges in medical treatment, as they can lead to increased morbidity, mortality, and healthcare costs. The overuse and misuse of antimicrobial agents, as well as poor infection control practices, contribute to the development and dissemination of drug-resistant strains. To address this issue, it is crucial to promote prudent use of antimicrobials, enhance surveillance and monitoring of resistance patterns, invest in research and development of new antimicrobial agents, and strengthen infection prevention and control measures.

Disulfiram is a medication used to treat chronic alcoholism. It works by inhibiting the enzyme acetaldehyde dehydrogenase, which is responsible for breaking down acetaldehyde, a toxic metabolite produced when alcohol is consumed. When a person taking disulfiram consumes alcohol, the buildup of acetaldehyde causes unpleasant symptoms such as flushing, nausea, palpitations, and shortness of breath, which can help discourage further alcohol use.

The medical definition of Disulfiram is:

A medication used in the treatment of chronic alcoholism, which works by inhibiting the enzyme acetaldehyde dehydrogenase, leading to an accumulation of acetaldehyde when alcohol is consumed, causing unpleasant symptoms that discourage further alcohol use. Disulfiram is available as a tablet for oral administration and is typically prescribed under medical supervision due to its potential for serious interactions with alcohol and other substances.

Methylcholanthrene is a polycyclic aromatic hydrocarbon that is used in research to induce skin tumors in mice. It is a potent carcinogen and mutagen, and exposure to it can increase the risk of cancer in humans. It is not typically found in medical treatments or therapies.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Molecular structure, in the context of biochemistry and molecular biology, refers to the arrangement and organization of atoms and chemical bonds within a molecule. It describes the three-dimensional layout of the constituent elements, including their spatial relationships, bond lengths, and angles. Understanding molecular structure is crucial for elucidating the functions and reactivities of biological macromolecules such as proteins, nucleic acids, lipids, and carbohydrates. Various experimental techniques, like X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM), are employed to determine molecular structures at atomic resolution, providing valuable insights into their biological roles and potential therapeutic targets.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Dithiothreitol (DTT) is a reducing agent, which is a type of chemical compound that breaks disulfide bonds between cysteine residues in proteins. DTT is commonly used in biochemistry and molecular biology research to prevent the formation of disulfide bonds during protein purification and manipulation.

Chemically, DTT is a small molecule with two sulfhydryl groups (-SH) that can donate electrons to oxidized cysteine residues in proteins, converting them to their reduced form (-S-H). This reaction reduces disulfide bonds and helps to maintain the solubility and stability of proteins.

DTT is also used as an antioxidant to prevent the oxidation of other molecules, such as DNA and enzymes, during experimental procedures. However, it should be noted that DTT can also reduce other types of bonds, including those in metal ions and certain chemical dyes, so its use must be carefully controlled and monitored.

DNA primers are short single-stranded DNA molecules that serve as a starting point for DNA synthesis. They are typically used in laboratory techniques such as the polymerase chain reaction (PCR) and DNA sequencing. The primer binds to a complementary sequence on the DNA template through base pairing, providing a free 3'-hydroxyl group for the DNA polymerase enzyme to add nucleotides and synthesize a new strand of DNA. This allows for specific and targeted amplification or analysis of a particular region of interest within a larger DNA molecule.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Chromatography, agarose is a type of chromatography technique that utilizes agarose gel as the stationary phase in the separation and analysis of biological molecules, such as DNA, RNA, and proteins. This method is commonly used in molecular biology for various applications, including DNA fragment separation, protein purification, and detection of specific nucleic acid sequences or proteins.

Agarose gel is a matrix made from agarose, a polysaccharide derived from seaweed. It has a porous structure with uniform pore size that allows for the size-based separation of molecules based on their ability to migrate through the gel under an electric field (in the case of electrophoresis) or by capillary action (in the case of capillary electrophoresis).

The charged molecules, such as DNA or proteins, interact with the agarose matrix and move through the gel at different rates depending on their size, charge, and shape. Smaller molecules can migrate more quickly through the pores of the gel, while larger molecules are retarded due to their inability to easily pass through the pores. This results in a separation of the molecules based on their physical properties, allowing for their analysis and characterization.

In summary, chromatography, agarose refers to the use of agarose gel as the stationary phase in the separation and analysis of biological molecules using various chromatography techniques, such as electrophoresis or capillary electrophoresis.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

Microsomes are subcellular membranous vesicles that are obtained as a byproduct during the preparation of cellular homogenates. They are not naturally occurring structures within the cell, but rather formed due to fragmentation of the endoplasmic reticulum (ER) during laboratory procedures. Microsomes are widely used in various research and scientific studies, particularly in the fields of biochemistry and pharmacology.

Microsomes are rich in enzymes, including the cytochrome P450 system, which is involved in the metabolism of drugs, toxins, and other xenobiotics. These enzymes play a crucial role in detoxifying foreign substances and eliminating them from the body. As such, microsomes serve as an essential tool for studying drug metabolism, toxicity, and interactions, allowing researchers to better understand and predict the effects of various compounds on living organisms.

Peptidyl transferase is not a medical term per se, but rather a biochemical term used to describe an enzymatic function or activity. It is often mentioned in the context of molecular biology, protein synthesis, and ribosome structure.

Peptidyl transferase refers to the catalytic activity of ribosomes that facilitates the formation of peptide bonds between amino acids during protein synthesis. More specifically, peptidyl transferase is responsible for transferring the peptidyl group (the growing polypeptide chain) from the acceptor site (A-site) to the donor site (P-site) of the ribosome, creating a new peptide bond and elongating the polypeptide chain. This activity occurs within the large subunit of the ribosome, near the peptidyl transferase center (PTC).

While it is often attributed to the ribosomal RNA (rRNA) component of the ribosome, recent research suggests that both rRNA and specific ribosomal proteins contribute to this enzymatic activity.

N-Acetylglucosaminyltransferases (GlcNAc transferases) are a group of enzymes that play a crucial role in the post-translational modification of proteins by adding N-acetylglucosamine (GlcNAc) to specific amino acids in a protein sequence. These enzymes catalyze the transfer of GlcNAc from a donor molecule, typically UDP-GlcNAc, to acceptor proteins, which can be other glycoproteins or proteins without any prior glycosylation.

The addition of N-acetylglucosamine by these enzymes is an essential step in the formation of complex carbohydrate structures called N-linked glycans, which are attached to asparagine residues within the protein sequence. The process of adding GlcNAc can occur in different ways, leading to various types of N-glycan structures, such as oligomannose, hybrid, and complex types.

There are several classes of N-Acetylglucosaminyltransferases (GnTs) based on their substrate specificity and the type of glycosidic linkage they form:

1. GnT I (MGAT1): Transfers GlcNAc to the α1,6 position of the mannose residue in the chitobiose core of N-linked glycans, initiating the formation of complex-type structures.
2. GnT II (MGAT2): Adds a second GlcNAc residue to the β1,4 position of the mannose residue at the non-reducing end of the chitobiose core, forming bi-antennary N-glycans.
3. GnT III (MGAT3): Transfers GlcNAc to the β1,4 position of the mannose residue in the chitobiose core, creating a branching point for further glycosylation and leading to tri- or tetra-antennary N-glycans.
4. GnT IV (MGAT4): Adds GlcNAc to the β1,4 position of the mannose residue at the non-reducing end of antennae, forming multi-branched complex-type structures.
5. GnT V (MGAT5): Transfers GlcNAc to the β1,6 position of the mannose residue in the chitobiose core, leading to hybrid and complex-type N-glycans with bisecting GlcNAc.
6. GnT VI (MGAT6): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
7. GnT VII (MGAT7): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
8. GnT VIII (MGAT8): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
9. GnT IX (MGAT9): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
10. GnT X (MGAT10): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
11. GnT XI (MGAT11): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
12. GnT XII (MGAT12): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
13. GnT XIII (MGAT13): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
14. GnT XIV (MGAT14): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
15. GnT XV (MGAT15): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
16. GnT XVI (MGAT16): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
17. GnT XVII (MGAT17): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
18. GnT XVIII (MGAT18): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
19. GnT XIX (MGAT19): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
20. GnT XX (MGAT20): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
21. GnT XXI (MGAT21): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
22. GnT XXII (MGAT22): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
23. GnT XXIII (MGAT23): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
24. GnT XXIV (MGAT24): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
25. GnT XXV (MGAT25): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
26. GnT XXVI (MGAT26): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
27. GnT XXVII (MGAT27): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
28. GnT XXVIII (MGAT28): Adds GlcNAc to the α1,3 position of the mannose residue at the non-reducing end of antennae, forming a-linked poly-N-acetyllactosamine structures.
29. GnT XXIX (MGAT29): Transfers GlcNAc to the β1,6 position of the N-acetylglucosamine residue in complex-type N-glycans, forming i-antigen structures.
30. GnT XXX (MG

Protein engineering is a branch of molecular biology that involves the modification of proteins to achieve desired changes in their structure and function. This can be accomplished through various techniques, including site-directed mutagenesis, gene shuffling, directed evolution, and rational design. The goal of protein engineering may be to improve the stability, activity, specificity, or other properties of a protein for therapeutic, diagnostic, industrial, or research purposes. It is an interdisciplinary field that combines knowledge from genetics, biochemistry, structural biology, and computational modeling.

Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.

For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Selenium is a trace element that is essential for the proper functioning of the human body. According to the medical definitions provided by the National Institutes of Health (NIH), selenium is a component of several major metabolic pathways, including thyroid hormone metabolism, antioxidant defense systems, and immune function.

Selenium is found in a variety of foods, including nuts (particularly Brazil nuts), cereals, fish, and meat. It exists in several forms, with selenomethionine being the most common form found in food. Other forms include selenocysteine, which is incorporated into proteins, and selenite and selenate, which are inorganic forms of selenium.

The recommended dietary allowance (RDA) for selenium is 55 micrograms per day for adults. While selenium deficiency is rare, chronic selenium deficiency can lead to conditions such as Keshan disease, a type of cardiomyopathy, and Kaschin-Beck disease, which affects the bones and joints.

It's important to note that while selenium is essential for health, excessive intake can be harmful. High levels of selenium can cause symptoms such as nausea, vomiting, hair loss, and neurological damage. The tolerable upper intake level (UL) for selenium is 400 micrograms per day for adults.

Biotransformation is the metabolic modification of a chemical compound, typically a xenobiotic (a foreign chemical substance found within an living organism), by a biological system. This process often involves enzymatic conversion of the parent compound to one or more metabolites, which may be more or less active, toxic, or mutagenic than the original substance.

In the context of pharmacology and toxicology, biotransformation is an important aspect of drug metabolism and elimination from the body. The liver is the primary site of biotransformation, but other organs such as the kidneys, lungs, and gastrointestinal tract can also play a role.

Biotransformation can occur in two phases: phase I reactions involve functionalization of the parent compound through oxidation, reduction, or hydrolysis, while phase II reactions involve conjugation of the metabolite with endogenous molecules such as glucuronic acid, sulfate, or acetate to increase its water solubility and facilitate excretion.

Carcinogens are agents (substances or mixtures of substances) that can cause cancer. They may be naturally occurring or man-made. Carcinogens can increase the risk of cancer by altering cellular DNA, disrupting cellular function, or promoting cell growth. Examples of carcinogens include certain chemicals found in tobacco smoke, asbestos, UV radiation from the sun, and some viruses.

It's important to note that not all exposures to carcinogens will result in cancer, and the risk typically depends on factors such as the level and duration of exposure, individual genetic susceptibility, and lifestyle choices. The International Agency for Research on Cancer (IARC) classifies carcinogens into different groups based on the strength of evidence linking them to cancer:

Group 1: Carcinogenic to humans
Group 2A: Probably carcinogenic to humans
Group 2B: Possibly carcinogenic to humans
Group 3: Not classifiable as to its carcinogenicity to humans
Group 4: Probably not carcinogenic to humans

This information is based on medical research and may be subject to change as new studies become available. Always consult a healthcare professional for medical advice.

'Structural homology' in the context of proteins refers to the similarity in the three-dimensional structure of proteins that are not necessarily related by sequence. This similarity arises due to the fact that these proteins have a common evolutionary ancestor or because they share a similar function and have independently evolved to adopt a similar structure. The structural homology is often identified using bioinformatics tools, such as fold recognition algorithms, that compare the three-dimensional structures of proteins to identify similarities. This concept is important in understanding protein function and evolution, as well as in the design of new drugs and therapeutic strategies.

Insecticide resistance is a genetic selection process in insect populations that allows them to survive and reproduce despite exposure to insecticides. It's the result of changes in the genetic makeup of insects, which can be caused by natural selection when insecticides are used repeatedly. Over time, this leads to the prevalence of genes that provide resistance to the insecticide, making the pest control methods less effective. Insecticide resistance is a significant challenge in public health and agriculture, as it can reduce the efficacy of interventions aimed at controlling disease-carrying insects or protecting crops from pests.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Epoxy compounds, also known as epoxy resins, are a type of thermosetting polymer characterized by the presence of epoxide groups in their molecular structure. An epoxide group is a chemical functional group consisting of an oxygen atom double-bonded to a carbon atom, which is itself bonded to another carbon atom.

Epoxy compounds are typically produced by reacting a mixture of epichlorohydrin and bisphenol-A or other similar chemicals under specific conditions. The resulting product is a two-part system consisting of a resin and a hardener, which must be mixed together before use.

Once the two parts are combined, a chemical reaction takes place that causes the mixture to cure or harden into a solid material. This curing process can be accelerated by heat, and once fully cured, epoxy compounds form a strong, durable, and chemically resistant material that is widely used in various industrial and commercial applications.

In the medical field, epoxy compounds are sometimes used as dental restorative materials or as adhesives for bonding medical devices or prosthetics. However, it's important to note that some people may have allergic reactions to certain components of epoxy compounds, so their use must be carefully evaluated and monitored in a medical context.

Tissue distribution, in the context of pharmacology and toxicology, refers to the way that a drug or xenobiotic (a chemical substance found within an organism that is not naturally produced by or expected to be present within that organism) is distributed throughout the body's tissues after administration. It describes how much of the drug or xenobiotic can be found in various tissues and organs, and is influenced by factors such as blood flow, lipid solubility, protein binding, and the permeability of cell membranes. Understanding tissue distribution is important for predicting the potential effects of a drug or toxin on different parts of the body, and for designing drugs with improved safety and efficacy profiles.

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

Tyrosine is an non-essential amino acid, which means that it can be synthesized by the human body from another amino acid called phenylalanine. Its name is derived from the Greek word "tyros," which means cheese, as it was first isolated from casein, a protein found in cheese.

Tyrosine plays a crucial role in the production of several important substances in the body, including neurotransmitters such as dopamine, norepinephrine, and epinephrine, which are involved in various physiological processes, including mood regulation, stress response, and cognitive functions. It also serves as a precursor to melanin, the pigment responsible for skin, hair, and eye color.

In addition, tyrosine is involved in the structure of proteins and is essential for normal growth and development. Some individuals may require tyrosine supplementation if they have a genetic disorder that affects tyrosine metabolism or if they are phenylketonurics (PKU), who cannot metabolize phenylalanine, which can lead to elevated tyrosine levels in the blood. However, it is important to consult with a healthcare professional before starting any supplementation regimen.

ADP Ribose Transferases are a group of enzymes that catalyze the transfer of ADP-ribose groups from donor molecules, such as NAD+ (nicotinamide adenine dinucleotide), to specific acceptor molecules. This transfer process plays a crucial role in various cellular processes, including DNA repair, gene expression regulation, and modulation of protein function.

The reaction catalyzed by ADP Ribose Transferases can be represented as follows:

Donor (NAD+ or NADP+) + Acceptor → Product (NR + ADP-ribosylated acceptor)

There are two main types of ADP Ribose Transferases based on their function and the type of modification they perform:

1. Poly(ADP-ribose) polymerases (PARPs): These enzymes add multiple ADP-ribose units to a single acceptor protein, forming long, linear, or branched chains known as poly(ADP-ribose) (PAR). PARylation is involved in DNA repair, genomic stability, and cell death pathways.
2. Monomeric ADP-ribosyltransferases: These enzymes transfer a single ADP-ribose unit to an acceptor protein, which is called mono(ADP-ribosyl)ation. This modification can regulate protein function, localization, and stability in various cellular processes, such as signal transduction, inflammation, and stress response.

Dysregulation of ADP Ribose Transferases has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of these enzymes is essential for developing novel therapeutic strategies to target these conditions.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

A kidney, in medical terms, is one of two bean-shaped organs located in the lower back region of the body. They are essential for maintaining homeostasis within the body by performing several crucial functions such as:

1. Regulation of water and electrolyte balance: Kidneys help regulate the amount of water and various electrolytes like sodium, potassium, and calcium in the bloodstream to maintain a stable internal environment.

2. Excretion of waste products: They filter waste products from the blood, including urea (a byproduct of protein metabolism), creatinine (a breakdown product of muscle tissue), and other harmful substances that result from normal cellular functions or external sources like medications and toxins.

3. Endocrine function: Kidneys produce several hormones with important roles in the body, such as erythropoietin (stimulates red blood cell production), renin (regulates blood pressure), and calcitriol (activated form of vitamin D that helps regulate calcium homeostasis).

4. pH balance regulation: Kidneys maintain the proper acid-base balance in the body by excreting either hydrogen ions or bicarbonate ions, depending on whether the blood is too acidic or too alkaline.

5. Blood pressure control: The kidneys play a significant role in regulating blood pressure through the renin-angiotensin-aldosterone system (RAAS), which constricts blood vessels and promotes sodium and water retention to increase blood volume and, consequently, blood pressure.

Anatomically, each kidney is approximately 10-12 cm long, 5-7 cm wide, and 3 cm thick, with a weight of about 120-170 grams. They are surrounded by a protective layer of fat and connected to the urinary system through the renal pelvis, ureters, bladder, and urethra.

Intramolecular oxidoreductases are a specific class of enzymes that catalyze the transfer of electrons within a single molecule, hence the term "intramolecular." These enzymes are involved in oxidoreduction reactions, where one part of the molecule is oxidized (loses electrons) and another part is reduced (gains electrons). This process allows for the rearrangement or modification of functional groups within the molecule.

The term "oxidoreductase" refers to enzymes that catalyze oxidation-reduction reactions, which are also known as redox reactions. These enzymes play a crucial role in various biological processes, including energy metabolism, detoxification, and biosynthesis.

It's important to note that intramolecular oxidoreductases should not be confused with intermolecular oxidoreductases, which catalyze redox reactions between two separate molecules.

An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.

Acyltransferases are a group of enzymes that catalyze the transfer of an acyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydrogen atom) from one molecule to another. This transfer involves the formation of an ester bond between the acyl group donor and the acyl group acceptor.

Acyltransferases play important roles in various biological processes, including the biosynthesis of lipids, fatty acids, and other metabolites. They are also involved in the detoxification of xenobiotics (foreign substances) by catalyzing the addition of an acyl group to these compounds, making them more water-soluble and easier to excrete from the body.

Examples of acyltransferases include serine palmitoyltransferase, which is involved in the biosynthesis of sphingolipids, and cholesteryl ester transfer protein (CETP), which facilitates the transfer of cholesteryl esters between lipoproteins.

Acyltransferases are classified based on the type of acyl group they transfer and the nature of the acyl group donor and acceptor molecules. They can be further categorized into subclasses based on their sequence similarities, three-dimensional structures, and evolutionary relationships.

Farnesyltranstransferase (FTase) is an enzyme that plays a role in the post-translational modification of proteins, specifically by adding a farnesyl group to certain protein substrates. This process, known as farnesylation, is essential for the proper localization and function of many proteins, including Ras family GTPases, which are involved in signal transduction pathways that regulate cell growth, differentiation, and survival.

FTase catalyzes the transfer of a farnesyl group from farnesyl pyrophosphate (FPP) to a cysteine residue near the C-terminus of its protein substrates. This modification allows the protein to interact with membranes and other cellular structures, which is critical for their function. Inhibitors of FTase have been developed as potential therapeutic agents for cancer and other diseases associated with aberrant Ras signaling.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Acetylcysteine is a medication that is used for its antioxidant effects and to help loosen thick mucus in the lungs. It is commonly used to treat conditions such as chronic bronchitis, emphysema, and cystic fibrosis. Acetylcysteine is also known by the brand names Mucomyst and Accolate. It works by thinning and breaking down mucus in the airways, making it easier to cough up and clear the airways. Additionally, acetylcysteine is an antioxidant that helps to protect cells from damage caused by free radicals. It is available as a oral tablet, liquid, or inhaled medication.

Viscosity is a physical property of a fluid that describes its resistance to flow. In medical terms, viscosity is often discussed in relation to bodily fluids such as blood or synovial fluid (found in joints). The unit of measurement for viscosity is the poise, although it is more commonly expressed in millipascals-second (mPa.s) in SI units. Highly viscous fluids flow more slowly than less viscous fluids. Changes in the viscosity of bodily fluids can have significant implications for health and disease; for example, increased blood viscosity has been associated with cardiovascular diseases, while decreased synovial fluid viscosity can contribute to joint pain and inflammation in conditions like osteoarthritis.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

A chemical model is a simplified representation or description of a chemical system, based on the laws of chemistry and physics. It is used to explain and predict the behavior of chemicals and chemical reactions. Chemical models can take many forms, including mathematical equations, diagrams, and computer simulations. They are often used in research, education, and industry to understand complex chemical processes and develop new products and technologies.

For example, a chemical model might be used to describe the way that atoms and molecules interact in a particular reaction, or to predict the properties of a new material. Chemical models can also be used to study the behavior of chemicals at the molecular level, such as how they bind to each other or how they are affected by changes in temperature or pressure.

It is important to note that chemical models are simplifications of reality and may not always accurately represent every aspect of a chemical system. They should be used with caution and validated against experimental data whenever possible.

The Cytochrome P-450 (CYP450) enzyme system is a group of enzymes found primarily in the liver, but also in other organs such as the intestines, lungs, and skin. These enzymes play a crucial role in the metabolism and biotransformation of various substances, including drugs, environmental toxins, and endogenous compounds like hormones and fatty acids.

The name "Cytochrome P-450" refers to the unique property of these enzymes to bind to carbon monoxide (CO) and form a complex that absorbs light at a wavelength of 450 nm, which can be detected spectrophotometrically.

The CYP450 enzyme system is involved in Phase I metabolism of xenobiotics, where it catalyzes oxidation reactions such as hydroxylation, dealkylation, and epoxidation. These reactions introduce functional groups into the substrate molecule, which can then undergo further modifications by other enzymes during Phase II metabolism.

There are several families and subfamilies of CYP450 enzymes, each with distinct substrate specificities and functions. Some of the most important CYP450 enzymes include:

1. CYP3A4: This is the most abundant CYP450 enzyme in the human liver and is involved in the metabolism of approximately 50% of all drugs. It also metabolizes various endogenous compounds like steroids, bile acids, and vitamin D.
2. CYP2D6: This enzyme is responsible for the metabolism of many psychotropic drugs, including antidepressants, antipsychotics, and beta-blockers. It also metabolizes some endogenous compounds like dopamine and serotonin.
3. CYP2C9: This enzyme plays a significant role in the metabolism of warfarin, phenytoin, and nonsteroidal anti-inflammatory drugs (NSAIDs).
4. CYP2C19: This enzyme is involved in the metabolism of proton pump inhibitors, antidepressants, and clopidogrel.
5. CYP2E1: This enzyme metabolizes various xenobiotics like alcohol, acetaminophen, and carbon tetrachloride, as well as some endogenous compounds like fatty acids and prostaglandins.

Genetic polymorphisms in CYP450 enzymes can significantly affect drug metabolism and response, leading to interindividual variability in drug efficacy and toxicity. Understanding the role of CYP450 enzymes in drug metabolism is crucial for optimizing pharmacotherapy and minimizing adverse effects.

'Anopheles' is a genus of mosquitoes that are known for their role in transmitting malaria parasites to humans. These mosquitoes have a distinctive resting posture, with their abdomens raised and heads down, and they typically feed on human hosts at night. Only female Anopheles mosquitoes transmit the malaria parasite, as they require blood meals to lay eggs.

There are over 400 species of Anopheles mosquitoes worldwide, but only about 30-40 of these are considered significant vectors of human malaria. The distribution and behavior of these mosquitoes can vary widely depending on the specific species and geographic location.

Preventing and controlling the spread of malaria involves a variety of strategies, including the use of insecticide-treated bed nets, indoor residual spraying, antimalarial drugs, and vaccines. Public health efforts to reduce the burden of malaria have made significant progress in recent decades, but the disease remains a major global health challenge, particularly in sub-Saharan Africa.

An electron is a subatomic particle, symbol e-, with a negative electric charge. Electrons are fundamental components of atoms and are responsible for the chemical bonding between atoms to form molecules. They are located in an atom's electron cloud, which is the outermost region of an atom and contains negatively charged electrons that surround the positively charged nucleus.

Electrons have a mass that is much smaller than that of protons or neutrons, making them virtually weightless on the atomic scale. They are also known to exhibit both particle-like and wave-like properties, which is a fundamental concept in quantum mechanics. Electrons play a crucial role in various physical phenomena, such as electricity, magnetism, and chemical reactions.

F344 is a strain code used to designate an outbred stock of rats that has been inbreeded for over 100 generations. The F344 rats, also known as Fischer 344 rats, were originally developed at the National Institutes of Health (NIH) and are now widely used in biomedical research due to their consistent and reliable genetic background.

Inbred strains, like the F344, are created by mating genetically identical individuals (siblings or parents and offspring) for many generations until a state of complete homozygosity is reached, meaning that all members of the strain have identical genomes. This genetic uniformity makes inbred strains ideal for use in studies where consistent and reproducible results are important.

F344 rats are known for their longevity, with a median lifespan of around 27-31 months, making them useful for aging research. They also have a relatively low incidence of spontaneous tumors compared to other rat strains. However, they may be more susceptible to certain types of cancer and other diseases due to their inbred status.

It's important to note that while F344 rats are often used as a standard laboratory rat strain, there can still be some genetic variation between individual animals within the same strain, particularly if they come from different suppliers or breeding colonies. Therefore, it's always important to consider the source and history of any animal model when designing experiments and interpreting results.

Immunoblotting, also known as western blotting, is a laboratory technique used in molecular biology and immunogenetics to detect and quantify specific proteins in a complex mixture. This technique combines the electrophoretic separation of proteins by gel electrophoresis with their detection using antibodies that recognize specific epitopes (protein fragments) on the target protein.

The process involves several steps: first, the protein sample is separated based on size through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Next, the separated proteins are transferred onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric field. The membrane is then blocked with a blocking agent to prevent non-specific binding of antibodies.

After blocking, the membrane is incubated with a primary antibody that specifically recognizes the target protein. Following this, the membrane is washed to remove unbound primary antibodies and then incubated with a secondary antibody conjugated to an enzyme such as horseradish peroxidase (HRP) or alkaline phosphatase (AP). The enzyme catalyzes a colorimetric or chemiluminescent reaction that allows for the detection of the target protein.

Immunoblotting is widely used in research and clinical settings to study protein expression, post-translational modifications, protein-protein interactions, and disease biomarkers. It provides high specificity and sensitivity, making it a valuable tool for identifying and quantifying proteins in various biological samples.

Sequence homology in nucleic acids refers to the similarity or identity between the nucleotide sequences of two or more DNA or RNA molecules. It is often used as a measure of biological relationship between genes, organisms, or populations. High sequence homology suggests a recent common ancestry or functional constraint, while low sequence homology may indicate a more distant relationship or different functions.

Nucleic acid sequence homology can be determined by various methods such as pairwise alignment, multiple sequence alignment, and statistical analysis. The degree of homology is typically expressed as a percentage of identical or similar nucleotides in a given window of comparison.

It's important to note that the interpretation of sequence homology depends on the biological context and the evolutionary distance between the sequences compared. Therefore, functional and experimental validation is often necessary to confirm the significance of sequence homology.

"Wistar rats" are a strain of albino rats that are widely used in laboratory research. They were developed at the Wistar Institute in Philadelphia, USA, and were first introduced in 1906. Wistar rats are outbred, which means that they are genetically diverse and do not have a fixed set of genetic characteristics like inbred strains.

Wistar rats are commonly used as animal models in biomedical research because of their size, ease of handling, and relatively low cost. They are used in a wide range of research areas, including toxicology, pharmacology, nutrition, cancer, cardiovascular disease, and behavioral studies. Wistar rats are also used in safety testing of drugs, medical devices, and other products.

Wistar rats are typically larger than many other rat strains, with males weighing between 500-700 grams and females weighing between 250-350 grams. They have a lifespan of approximately 2-3 years. Wistar rats are also known for their docile and friendly nature, making them easy to handle and work with in the laboratory setting.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Hydrogen peroxide (H2O2) is a colorless, odorless, clear liquid with a slightly sweet taste, although drinking it is harmful and can cause poisoning. It is a weak oxidizing agent and is used as an antiseptic and a bleaching agent. In diluted form, it is used to disinfect wounds and kill bacteria and viruses on the skin; in higher concentrations, it can be used to bleach hair or remove stains from clothing. It is also used as a propellant in rocketry and in certain industrial processes. Chemically, hydrogen peroxide is composed of two hydrogen atoms and two oxygen atoms, and it is structurally similar to water (H2O), with an extra oxygen atom. This gives it its oxidizing properties, as the additional oxygen can be released and used to react with other substances.

A "gene library" is not a recognized term in medical genetics or molecular biology. However, the closest concept that might be referred to by this term is a "genomic library," which is a collection of DNA clones that represent the entire genetic material of an organism. These libraries are used for various research purposes, such as identifying and studying specific genes or gene functions.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

A conserved sequence in the context of molecular biology refers to a pattern of nucleotides (in DNA or RNA) or amino acids (in proteins) that has remained relatively unchanged over evolutionary time. These sequences are often functionally important and are highly conserved across different species, indicating strong selection pressure against changes in these regions.

In the case of protein-coding genes, the corresponding amino acid sequence is deduced from the DNA sequence through the genetic code. Conserved sequences in proteins may indicate structurally or functionally important regions, such as active sites or binding sites, that are critical for the protein's activity. Similarly, conserved non-coding sequences in DNA may represent regulatory elements that control gene expression.

Identifying conserved sequences can be useful for inferring evolutionary relationships between species and for predicting the function of unknown genes or proteins.

Phenylalanine is an essential amino acid, meaning it cannot be produced by the human body and must be obtained through diet or supplementation. It's one of the building blocks of proteins and is necessary for the production of various molecules in the body, such as neurotransmitters (chemical messengers in the brain).

Phenylalanine has two forms: L-phenylalanine and D-phenylalanine. L-phenylalanine is the form found in proteins and is used by the body for protein synthesis, while D-phenylalanine has limited use in humans and is not involved in protein synthesis.

Individuals with a rare genetic disorder called phenylketonuria (PKU) must follow a low-phenylalanine diet or take special medical foods because they are unable to metabolize phenylalanine properly, leading to its buildup in the body and potential neurological damage.

Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.

Genotype, in genetics, refers to the complete heritable genetic makeup of an individual organism, including all of its genes. It is the set of instructions contained in an organism's DNA for the development and function of that organism. The genotype is the basis for an individual's inherited traits, and it can be contrasted with an individual's phenotype, which refers to the observable physical or biochemical characteristics of an organism that result from the expression of its genes in combination with environmental influences.

It is important to note that an individual's genotype is not necessarily identical to their genetic sequence. Some genes have multiple forms called alleles, and an individual may inherit different alleles for a given gene from each parent. The combination of alleles that an individual inherits for a particular gene is known as their genotype for that gene.

Understanding an individual's genotype can provide important information about their susceptibility to certain diseases, their response to drugs and other treatments, and their risk of passing on inherited genetic disorders to their offspring.

Molecular evolution is the process of change in the DNA sequence or protein structure over time, driven by mechanisms such as mutation, genetic drift, gene flow, and natural selection. It refers to the evolutionary study of changes in DNA, RNA, and proteins, and how these changes accumulate and lead to new species and diversity of life. Molecular evolution can be used to understand the history and relationships among different organisms, as well as the functional consequences of genetic changes.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Genetic polymorphism refers to the occurrence of multiple forms (called alleles) of a particular gene within a population. These variations in the DNA sequence do not generally affect the function or survival of the organism, but they can contribute to differences in traits among individuals. Genetic polymorphisms can be caused by single nucleotide changes (SNPs), insertions or deletions of DNA segments, or other types of genetic rearrangements. They are important for understanding genetic diversity and evolution, as well as for identifying genetic factors that may contribute to disease susceptibility in humans.

Reactive Oxygen Species (ROS) are highly reactive molecules containing oxygen, including peroxides, superoxide, hydroxyl radical, and singlet oxygen. They are naturally produced as byproducts of normal cellular metabolism in the mitochondria, and can also be generated by external sources such as ionizing radiation, tobacco smoke, and air pollutants. At low or moderate concentrations, ROS play important roles in cell signaling and homeostasis, but at high concentrations, they can cause significant damage to cell structures, including lipids, proteins, and DNA, leading to oxidative stress and potential cell death.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

Gel chromatography is a type of liquid chromatography that separates molecules based on their size or molecular weight. It uses a stationary phase that consists of a gel matrix made up of cross-linked polymers, such as dextran, agarose, or polyacrylamide. The gel matrix contains pores of various sizes, which allow smaller molecules to penetrate deeper into the matrix while larger molecules are excluded.

In gel chromatography, a mixture of molecules is loaded onto the top of the gel column and eluted with a solvent that moves down the column by gravity or pressure. As the sample components move down the column, they interact with the gel matrix and get separated based on their size. Smaller molecules can enter the pores of the gel and take longer to elute, while larger molecules are excluded from the pores and elute more quickly.

Gel chromatography is commonly used to separate and purify proteins, nucleic acids, and other biomolecules based on their size and molecular weight. It is also used in the analysis of polymers, colloids, and other materials with a wide range of applications in chemistry, biology, and medicine.

A multigene family is a group of genetically related genes that share a common ancestry and have similar sequences or structures. These genes are arranged in clusters on a chromosome and often encode proteins with similar functions. They can arise through various mechanisms, including gene duplication, recombination, and transposition. Multigene families play crucial roles in many biological processes, such as development, immunity, and metabolism. Examples of multigene families include the globin genes involved in oxygen transport, the immune system's major histocompatibility complex (MHC) genes, and the cytochrome P450 genes associated with drug metabolism.

The adrenal glands are a pair of endocrine glands that are located on top of the kidneys. Each gland has two parts: the outer cortex and the inner medulla. The adrenal cortex produces hormones such as cortisol, aldosterone, and androgens, which regulate metabolism, blood pressure, and other vital functions. The adrenal medulla produces catecholamines, including epinephrine (adrenaline) and norepinephrine (noradrenaline), which help the body respond to stress by increasing heart rate, blood pressure, and alertness.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

Malondialdehyde (MDA) is a naturally occurring organic compound that is formed as a byproduct of lipid peroxidation, a process in which free radicals or reactive oxygen species react with polyunsaturated fatty acids. MDA is a highly reactive aldehyde that can modify proteins, DNA, and other biomolecules, leading to cellular damage and dysfunction. It is often used as a marker of oxidative stress in biological systems and has been implicated in the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

Quaternary protein structure refers to the arrangement and interaction of multiple folded protein molecules in a multi-subunit complex. These subunits can be identical or different forms of the same protein or distinctly different proteins that associate to form a functional complex. The quaternary structure is held together by non-covalent interactions, such as hydrogen bonds, ionic bonds, and van der Waals forces. Understanding quaternary structure is crucial for comprehending the function, regulation, and assembly of many protein complexes involved in various cellular processes.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

Glutaredoxins (Grxs) are small, ubiquitous proteins that belong to the thioredoxin superfamily. They play a crucial role in maintaining the redox balance within cells by catalyzing the reversible reduction of disulfide bonds and mixed disulfides between protein thiols and low molecular weight compounds, using glutathione (GSH) as a reducing cofactor.

Glutaredoxins are involved in various cellular processes, such as:

1. DNA synthesis and repair
2. Protein folding and degradation
3. Antioxidant defense
4. Regulation of enzyme activities
5. Iron-sulfur cluster biogenesis

There are two main classes of glutaredoxins, Grx1 and Grx2, which differ in their active site sequences and functions. In humans, Grx1 is primarily located in the cytosol, while Grx2 is found in both the cytosol and mitochondria.

The medical relevance of glutaredoxins lies in their role as antioxidant proteins that protect cells from oxidative stress and maintain cellular redox homeostasis. Dysregulation of glutaredoxin function has been implicated in several pathological conditions, including neurodegenerative diseases, cancer, and aging-related disorders.

Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.

Mutagenesis is the process by which the genetic material (DNA or RNA) of an organism is changed in a way that can alter its phenotype, or observable traits. These changes, known as mutations, can be caused by various factors such as chemicals, radiation, or viruses. Some mutations may have no effect on the organism, while others can cause harm, including diseases and cancer. Mutagenesis is a crucial area of study in genetics and molecular biology, with implications for understanding evolution, genetic disorders, and the development of new medical treatments.

Galactosyltransferases are a group of enzymes that play a crucial role in the biosynthesis of glycoconjugates, which are complex carbohydrate structures found on the surface of many cell types. These enzymes catalyze the transfer of galactose, a type of sugar, to another molecule, such as another sugar or a lipid, to form a glycosidic bond.

Galactosyltransferases are classified based on the type of donor substrate they use and the type of acceptor substrate they act upon. For example, some galactosyltransferases use UDP-galactose as a donor substrate and transfer galactose to an N-acetylglucosamine (GlcNAc) residue on a protein or lipid, forming a lactosamine unit. Others may use different donor and acceptor substrates to form different types of glycosidic linkages.

These enzymes are involved in various biological processes, including cell recognition, signaling, and adhesion. Abnormalities in the activity of galactosyltransferases have been implicated in several diseases, such as congenital disorders of glycosylation, cancer, and inflammatory conditions. Therefore, understanding the function and regulation of these enzymes is important for developing potential therapeutic strategies for these diseases.

N-Acetylgalactosaminyltransferases (GalNAc-Ts) are a family of enzymes that play a crucial role in the process of protein glycosylation. Protein glycosylation is the attachment of carbohydrate groups, also known as glycans, to proteins. This modification significantly influences various biological processes such as protein folding, stability, trafficking, and recognition.

GalNAc-Ts specifically catalyze the transfer of N-acetylgalactosamine (GalNAc) from a donor molecule, UDP-GalNAc, to serine or threonine residues on acceptor proteins. This initial step of adding GalNAc to proteins is called mucin-type O-glycosylation and sets the stage for further glycan additions by other enzymes.

There are at least 20 different isoforms of GalNAc-Ts identified in humans, each with distinct substrate specificities, tissue distributions, and subcellular localizations. Aberrant expression or dysfunction of these enzymes has been implicated in various diseases, including cancer, where altered glycosylation patterns contribute to tumor progression and metastasis.

Glutathione transferases play a key role in catalyzing such reactions. Bacterial glutathione transferases of all classes are ... Without glutathione in its reduced form, glutathione transferases are not able to utilize it as a substrate in redox reactions ... Bacterial glutathione transferases (GSTs; EC 2.5.1.18) are part of a superfamily of enzymes that play a crucial role in ... Bacterial glutathione transferases are not detected in anaerobic bacteria or archaea. These antioxidant enzymes are a part of ...
Affinity chromatography Bacterial glutathione transferase Glutathione S-transferase Mu 1 Glutathione S-transferase, C-terminal ... Overview of Glutathione S-Transferases Glutathione+S-Transferase at the U.S. National Library of Medicine Medical Subject ... "Glutathione S-transferase pull-down assays using dehydrated immobilized glutathione resin". Analytical Biochemistry. 322 (2): ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles ...
... is an enzyme that in humans is encoded by the GSTA1 gene. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTA1 glutathione S-transferase A1". Knapen, MF; Mulder, TP; Bisseling, JG; Penders, RH; Peters, WH; Steegers, EA ... This gene encodes a glutathione S-transferase belonging to the alpha class. The alpha class genes, located in a cluster mapped ... 1988). "Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate ...
... (gene name GSTM1) is a human glutathione S-transferase. Cytosolic and membrane-bound forms of ... "Entrez Gene: GSTM1 glutathione S-transferase M1". Engel LS, Taioli E, Pfeiffer R, Garcia-Closas M, Marcus PM, Lan Q, et al. ( ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Glutathione S-transferase Mu 1 v t ... This gene encodes a cytoplasmic glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in ...
... is an enzyme that in humans is encoded by the MGST1 gene. The MAPEG family (Membrane- ... Cholon A, Giaccia AJ, Lewis AD (1992). "What role do glutathione S-transferases play in the cellular response to ionizing ... DeJong JL, Mohandas T, Tu CP (1990). "The gene for the microsomal glutathione S-transferase is on human chromosome 12". ... DeJong JL, Morgenstern R, Jörnvall H (1988). "Gene expression of rat and human microsomal glutathione S-transferases". J. Biol ...
... is a structural domain of glutathione S-transferase (GST). GST conjugates reduced ... "Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles ... Glutathione S-transferases form homodimers, but in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 ... In eukaryotes, glutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic compounds by ...
... a tool to measure the cellular glutathione redox potential Glutathione-ascorbate cycle Bacterial glutathione transferase ... Glutathione facilitates metabolism of xenobiotics. Glutathione S-transferase enzymes catalyze its conjugation to lipophilic ... Glutathione exists in reduced (GSH) and oxidized (GSSG) states. The ratio of reduced glutathione to oxidized glutathione within ... Glutathione enhances the function of citrulline as part of the nitric oxide cycle. It is a cofactor and acts on glutathione ...
Habig WH, Pabst MJ, Jakoby WB (1974). "Glutathione S-transferases. The first enzymatic step in mercapturic acid formation". J ... The molecule is conjugated to a single molecule of reduced glutathione which then absorbs at 340 nm. Affinity of CDNB for each ...
"Entrez Gene: GSTA3 glutathione S-transferase A3". Johansson AS, Mannervik B (2001). "Human glutathione transferase A3-3, a ... Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene. Cytosolic and membrane-bound forms of ... This gene encodes a glutathione S-transferase belonging to the alpha class genes that are located in a cluster mapped to ... Suzuki T, Johnston PN, Board PG (Mar 1994). "Structure and organization of the human alpha class glutathione S-transferase ...
Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene. Glutathione S-transferases (GSTs) are a ... "Entrez Gene: GSTP1 glutathione S-transferase pi". Cumming RC, Lightfoot J, Beard K, Youssoufian H, O'Brien PJ, Buchwald M (July ... The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant ... Wang T, Arifoglu P, Ronai Z, Tew KD (15 June 2001). "Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase ...
Glutathione S-transferase theta-1 is an enzyme that in humans is encoded by the GSTT1 gene. Glutathione S-transferase (GST) ... "Entrez Gene: GSTT1 glutathione S-transferase theta 1". v t e (Articles with short description, Short description matches ... "Chromosomal localization of the gene for the human theta class glutathione transferase (GSTT1)". Genomics. 33 (1): 121-3. doi: ... theta 1 (GSTT1) is a member of a superfamily of proteins that catalyze the conjugation of reduced glutathione to a variety of ...
... also possesses a glutathione S-transferase. Cunninghamella elegans is a microbial model of mammalian ... Cytochrome P450 monooxygenase, aryl sulfotransferase, glutathione S-transferase, UDP-glucuronosyltransferase, UDP- ... expression and characterization of a novel class glutathione S-transferase from the fungus Cunninghamella elegans". Biochemical ...
Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene. This gene encodes a member of the ... "Entrez Gene: GSTO1 glutathione S-transferase omega 1". Whitbread AK, Masoumi A, Tetlow N, Schmuck E, Coggan M, Board PG (2005 ... 2004). "Glutathione S-transferase omega-1 modifies age-at-onset of Alzheimer disease and Parkinson disease". Hum. Mol. Genet. ... 2007). "Glutathione S-transferase omega in the lung and sputum supernatants of COPD patients". Respir. Res. 8 (1): 48. doi: ...
Glutathione S-transferase M3 (brain), also known as GSTM2, is an enzyme which in humans is encoded by the GSTM99 gene. ... "Entrez Gene: GSTM3 glutathione S-transferase M3 (brain)". Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I (June ... This gene encodes a glutathione S-transferase that belongs to the mu class. The mu class of enzymes functions in the ... Gough AC, Zhong S, Wolf CR, Spurr NK (1993). "Chromosome assignment of the human glutathione S-transferase mu 3 gene (GSTM3) to ...
Microsomal glutathione S-transferase 2 is an enzyme that in humans is encoded by the MGST2 gene. The MAPEG (Membrane-Associated ... "Entrez Gene: MGST2 microsomal glutathione S-transferase 2". Jakobsson PJ, Morgenstern R, Mancini J, et al. (2000). "Membrane- ... 2001). "Human umbilical vein endothelial cells generate leukotriene C4 via microsomal glutathione S-transferase type 2 and ... 2006). "Systematic evaluation of association between the microsomal glutathione S-transferase 2 common variation and psoriasis ...
Glutathione S-transferase theta-2 is an enzyme that in humans is encoded by the GSTT2 gene. Glutathione S-transferase (GSTs) ... GSTT2 glutathione S-transferase theta 2". Hussey AJ, Hayes JD (1992). "Characterization of a human class-Theta glutathione S- ... 1996). "The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human". Biochem. J. ... de Bruin WC, Wagenmans MJ, Peters WH (2000). "Expression of glutathione S-transferase alpha, P1-1 and T1-1 in the human ...
Glutathione S-transferase omega-2 is an enzyme that in humans is encoded by the GSTO2 gene. Model organisms have been used in ... Morari EC, Lima AB, Bufalo NE, Leite JL, Granja F, Ward LS (Aug 2006). "Role of glutathione-S-transferase and codon 72 of P53 ... "Entrez Gene: GSTO2 glutathione S-transferase omega 2". Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput ... Leite JL, Morari EC, Granja F, Campos GM, Guilhen AC, Ward LS (Mar 2007). "Influence of the glutathione s-transferase gene ...
Microsomal glutathione S-transferase 3 is an enzyme that in humans is encoded by the MGST3 gene. The MAPEG (Membrane-Associated ... 2003). "Evaluation of the microsomal glutathione S-transferase 3 (MGST3) locus on 1q23 as a Type 2 diabetes susceptibility gene ... "Entrez Gene: MGST3 microsomal glutathione S-transferase 3". "Salmonella infection data for Mgst3". Wellcome Trust Sanger ... "Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase ...
Glutathione S-transferase Zeta 1 (also known as maleylacetoacetate isomerase) is an enzyme that in humans is encoded by the ... Glutathione S-transferase Zeta 1 (GSTZ1) has a predominantly hydrophobic dimer, just like many other GST members. It is ... Board PG, Baker RT, Chelvanayagam G, Jermiin LS (Dec 1997). "Zeta, a novel class of glutathione transferases in a range of ... "Entrez Gene: GSTZ1 glutathione transferase zeta 1 (maleylacetoacetate isomerase)". Polekhina G, Board PG, Blackburn AC, Parker ...
... can induce the enzyme glutathione S-transferase (GST). GST has been suggested to protect cells against oxidative ... Myricetin's pro-oxidative capabilities can also be seen in its ability to act as an inhibitory agent against glutathione ... reductase, which is responsible for regenerating glutathione, a scavenger of free radicals and peroxides. Myricetin is also ...
Soybeans naturally have a high tolerance to fomesafen, via metabolic disposal by glutathione S-transferase. As a result, soy is ... "Glutathione transferase activities toward herbicides used selectively in soybean". Pesticide Science. Wiley. 51 (2): 213-222. ...
Soybeans naturally have a high tolerance to acifluorfen and its salts, via metabolic disposal by glutathione S-transferase. It ... "Glutathione transferase activities toward herbicides used selectively in soybean". Pesticide Science. Wiley. 51 (2): 213-222. ...
... and bioinformatics studies of the human Kappa-class glutathione transferase predict a novel third glutathione transferase ... Glutathione S-transferase kappa 1 (GSTK1) is an enzyme that in humans is encoded by the GSTK1 gene which is located on ... It belongs to the superfamily of enzymes known as glutathione S-transferase (GST), which are mainly known for cellular ... Li J, Xia Z, Ding J (Sep 2005). "Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology ...
Plants use glutathione transferases as a means to segregate toxic metals from the rest of the cell. These glutathione ... Terminal transferase is one of the few DNA polymerases that can function without an RNA primer. The family of glutathione ... Glutathione transferases are currently being explored as targets for anti-cancer medications due to their role in drug ... Further, glutathione transferase genes have been investigated due to their ability to prevent oxidative damage and have shown ...
Protein tag Fluorescent glucose biosensors Glutathione S-transferase Duan, Xiaoqun; Hall, Jason A; Nikaido, Hiroshi; Quiocho, ...
... or glutathione S-transferase II) is an enzyme that converts leukotriene A4 and glutathione to create leukotriene C4. This is a ... This protein is remotely related to microsomal glutathione S-transferase. The MAPEG (Membrane-Associated Proteins in Eicosanoid ... a homodimeric glutathione S-transferase composed of 18-kDa subunits". Proc. Natl. Acad. Sci. U.S.A. 90 (5): 2015-9. Bibcode: ... 2000). "Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily". Am. J ...
Shi, B.; Stevenson, R.; Campopiano, D. J.; Greaney, M. F. (Jul 2006). "Discovery of glutathione S-transferase inhibitors using ...
FMO4 (vimentin/dimethylalanine monooxygenase 4) and GSTM4 (glutathione transferase M4). The expression of Class III β-tubulin ...
Kotb, Magd A. (March 2015). "Evidence of Disruption of p53 and Glutathione S Transferase Pi in Extrahepatic Biliary Atresia in ... The babies have homozygous deficiency of glutathione S transferase (GST) M1. The aflatoxin damaged liver cells and bile duct ... Kotb, Magd A (March 2015). "Glutathione S Transferase M1 Polymorphism in Extrahepatic Biliary Atresia" (PDF). The Medical ... proven to be as a result of aflatoxin induced cholangiopathy acquired prenatally in infants who have glutathione S transferase ...
"Incorporation of Tellurocysteine into Glutathione Transferase Generates High Glutathione Peroxidase Efficiency". Angewandte ... When incorporated into glutathione transferase, tellurocysteine efficiently inhibited aminoacylation and increased the ... efficiency of glutathione peroxidase. L-Tellurocystine has been prepared in low yield from a protected form of 3-iodoalanine. ...
Glutathione transferases play a key role in catalyzing such reactions. Bacterial glutathione transferases of all classes are ... Without glutathione in its reduced form, glutathione transferases are not able to utilize it as a substrate in redox reactions ... Bacterial glutathione transferases (GSTs; EC 2.5.1.18) are part of a superfamily of enzymes that play a crucial role in ... Bacterial glutathione transferases are not detected in anaerobic bacteria or archaea. These antioxidant enzymes are a part of ...
... shown that certain GST isozymes can regulate mitogen-activated protein kinases or can facilitate the addition of glutathione to ... The super family of glutathione S-transferases (GSTs) is composed of multiple isozymes with significant evidence of functional ... Glutathione S-transferase polymorphisms: cancer incidence and therapy. *C C McIlwain1, ... Glutathione S-transferase Mu 2 inhibits hepatic steatosis via ASK1 suppression *Yi Jin ...
... membrane associated proteins in eicosanoid and glutathione metabolism), defined according to enzymatic activities, sequence ... Microsomal glutathione transferase 1 (MGST1) is a member of the MAPEG family ( ... Microsomal glutathione transferase 1 in cancer and the regulation of ferroptosis Adv Cancer Res. 2023:160:107-132. doi: 10.1016 ... MGST1 has both glutathione transferase and peroxidase activities. Each is based on stabilizing the GSH thiolate in the same ...
Crystal structure of glutathione transferase F7 from Populus trichocarpa ... Glutathione S-transferase family protein. A, B. 216. Populus trichocarpa. Mutation(s): 0 Gene Names: POPTR_0002s20900g, POPTR_ ... and F8 displayed a thiol transferase activity in addition to the usual glutathione transferase and peroxidase activities. From ... The glutathione transferase (GST) gene family is divided into 14 classes in photosynthetic organisms. Among them, the Phi class ...
... ... GLUTATHIONE S-TRANSFERASE1-Menaphthyl Glutathione ConjugateSulfate Ion ...
View our 4 Glutathione S-Transferase pi 1/GSTP1 products for your research including Glutathione S-Transferase pi 1/GSTP1 ...
Glutathione S-Transferase, GST, Glutathione S-transferase class-mu 28 kDa isozyme, GST 28, EC 2.5.1.18, Sj28GST, Sj28 antigen. ... Antioxidant enzyme Glutathione S- Transferase (GST) is thought to do the primary cellular defense mechanism against reactive ... GST reduces lipid hydroperoxides through its Se-independent glutathione peroxidase activity. The enzyme also detoxifies lipid ... with reduced glutathione per minute at pH-6.5 at 25C. ...
... 24 GSTU24) - Gentaur.com - Product info ... glutathione S-transferase TAU 24; Glutathione S-transferase U24; glutathione S-transferase TAU 24; GST class-tau member 24] ... Arabidopsis thaliana Glutathione S-transferase (class tau) 24; ATGSTU24; F20D23.13; F20D23_13; glutathione S-transferase TAU 24 ...
Glutathione may be useful for monitoring melatonins protective role on cell damage. ... The effect of melatonin on glutathione and glutathione transferase and glutathione peroxidase activities in the mouse liver and ... Objectives: The changes in reduced glutathione (GSH), activity of glutathione transferase (GST) and glutathione peroxidase ( ... Results: Melatonin caused an increase in glutathione level, the activity of glutathione peroxidase as well as glutathione ...
... the cytosolic glutathione transferase (cGST) fold. A total of 39 proteins were found, including the alpha-, mu-, pi-, sigma-, ... the cytosolic glutathione transferase (cGST) fold. A total of 39 proteins were found, including the alpha-, mu-, pi-, sigma-, ...
Cytochrome P450-mediated bioactivation of mefenamic acid to quinoneimine intermediates and inactivation by human glutathione S- ... transferases. Download Prime PubMed App to iPhone, iPad, or Android ... Effect of human glutathione S-transferases on glutathione-dependent inactivation of cytochrome P450-dependent reactive ... Role of human glutathione S-transferases in the inactivation of reactive metabolites of clozapine. ...
Glutathione S Transferase Alpha 1) ELISA Kit from Gentaur Elisa Kits. Cat Number: G-EC-03989. USA, UK & Europe Distribution. ... Human GSTα1 (Glutathione S Transferase Alpha 1) ELISA Kit , G-EC-03989. Gentaur Elisa ... Human GSTα1 (Glutathione S Transferase Alpha 1) ELISA Kit , G-EC-03989 ... Human GSTα1 (Glutathione S Transferase Alpha 1) ELISA Kit , G-EC-03989 , Gentaur Elisa Kits ...
Influence of glutathione-S-transferase (GSTM1, GSTP1, GSTT1) and cytochrome p450 (CYP1A1, CYP2D6) polymorphisms on numbers of ... Influence of glutathione-S-transferase (GSTM1, GSTP1, GSTT1) and cytochrome p450 (CYP1A1, CYP2D6) polymorphisms on numbers of ... and glutathione-S-transferase (GST) enzymes influenced the numbers of BCCs in sporadic BCC cases. ...
S-transferase (GST). We have isolated a cDNA encoding the human anionic glutathione-S-transferase, GSTπ-1, from a cDNA library ... Expression of Anionic Glutathione-S-transferase and P-Glycoprotein Genes in Human Tissues and Tumors Jeffrey A. Moscow; Jeffrey ... Expression of Anionic Glutathione-S-transferase and P-Glycoprotein Genes in Human Tissues and Tumors. Cancer Res 15 March 1989 ... among these changes is a significant increase in the activity of the anionic isozyme of glutathione- ...
Biophysical methods were used to elucidate the mechanism and molecular consequences of S-nitrosation of glutathione transferase ... Biophysical methods were used to elucidate the mechanism and molecular consequences of S-nitrosation of glutathione transferase ...
... Jennifer Campbell jcampbell ,@t, vdxpathology.com Wed Dec 16 10: ...
A recent clinical study has focused on: 1- the interaction between genetic variants of glutathione S-transferases M1 and T1 ( ... Smoking, genetic polymorphisms of glutathione S-transferases and biological indices of inflammation and cellular adhesion in ... glutathione S-transferase polymorphism. inflammation. molecule. smoking. URI: http://hdl.handle.net/2003/25637. http://dx.doi. ...
Effect of Alcohol Withdrawl on Glutathione S-transferase, Total Antioxidant Capacity and Amylase in Blood and Saliva of Alcohol ...
This study examined the association between overall survival and Glutathione S-transferase Pi (GST Pi) expression and genetic ... Glutathione S-transferase Pi (GST Pi) is found in the cell nucleus, cytoplasm and mitochondria of a wide range of normal and ... Doğru-Abbasoğlu S, Mutlu-Turkoğlu Ü, Türkoğlu S, Erbil Y, Barbaros U, Uysal M, Aykaç-Toker G: Glutathione S-transferase-pi in ... Glutathione S-transferase Pi expression predicts response to adjuvant chemotherapy for stage C colon cancer: a matched ...
Methylated Glutathione S-transferase 1 (mGSTP1) is a potential plasma free DNA epigenetic marker of prognosis and response to ... Methylated Glutathione S-transferase 1 (mGSTP1) is a potential plasma free DNA epigenetic marker of prognosis and response to ... Methylated Glutathione S-transferase 1 (mGSTP1) is a potential plasma free DNA epigenetic marker of prognosis and response to ... Methylated Glutathione S-transferase 1 (mGSTP1) is a potential plasma free DNA epigenetic marker of prognosis and response to ...
glutathione S-transferase TAU 1. glutathione S-transferase TAU 1,. GLUTATHIONE S-TRANSFERASE 19,. glutathione S-transferase TAU ... glutathione S-transferase TAU 19. A. THALIANA GLUTATHIONE. S-TRANSFERASE TAU 19, GLUTATHIONE. TRANSFERASE 8, glutathione. S- ... glutathione S-transferase TAU 8. glutathione S-transferase TAU 8,. glutathione S-transferase TAU 8. 0.86. 0.32. -0.3. ... glutathione S-transferase TAU 22. glutathione S-transferase TAU 22,. glutathione S-transferase TAU 22. 0.85. 0.29. -0.32. ...
Estimation of Glutathione-S-transferase activity. Determination of Glutathione-S-transferase (GST) activity was carried out in ... Glutathione-S-Transferase (GST, µmol CDNB-GSH conjugate/min) (E) Catalase (U/mg protein/min) and (F). Malondialdehyde (MDA, ... Habig, W. H., Pabst, M. J. & Jakoby, W. B. Glutathione S-transferases the first enzymatic step in mercapturic acid formation. J ... The reaction mixture contained 500 µl of 0.1 M phosphate buffer (pH 6.0), 200 µl of 10 Mm reduced glutathione, 150 µl of 10 mM ...
Glutathione-s-transferase (GST). GST represents a family of cytosolic, microsomal, and membrane-bound enzymes. The GST alpha ... Distribution of glutathione S-transferase isoenzymes in human kidney: basis for possible markers of renal injury. J Clin Pathol ... along with alpha-glutathione-s-transferase (GST), were able to predict future development of stages 1 and 3 AKI. [44] In a ...
Decrease Quantity of Glutathione-S-Transferase (GST) Activity Assay Kit(DTNB method) Increase Quantity of Glutathione-S- ... Detection principle Glutathione S-transferase is a kind of enzyme related to liver detoxification, which is often used as an ...
Polymorphism in glutathione S-transferase P1 is associated with susceptibility to chemotherapy-induced leukemia.. J M Allan, C ... Glutathione S-transferases (GSTs) detoxify potentially mutagenic and toxic DNA-reactive electrophiles, including metabolites of ...
In this report, we describe the glutathione transferase (GST) gene family in the dengue vector Aedes aegypti and suggest a ... glutathione transferase insecticide resistance aedes aegypti anopheles gambiae ddt heme multiple sequence alignment s- ... The Aedes aegypti glutathione transferase family. Insect Biochemistry and Molecular Biology, Vol 37, Issue 10, pp. 1026-1035. ... transferase anopheles-gambiae insecticide-resistance supergene family identification expression binding vector ddt. ...
Gullner, G. and Kőmíves, T. (2006) Defense Reactions of Infected Plants: Roles of Glutathione and Glutathione S-Transferase ... Defense Reactions of Infected Plants: Roles of Glutathione and Glutathione S-Transferase Enzymes ... Several lines of evidence suggest that glutathione S-transferase (GST) isoenzymes also have an important role in plant disease ... In recent years, the importance of the endogenous plant tripeptide glutathione (GSH) has been increasingly recognized in plant- ...
You are here: Home1 / ELISA Kits2 / Goat Glutathione S Transferase Alpha 2 ELISA Kit ... Goat Cl+-transportingÿATPase ELISA KitGoat Glutathione S Transferase Alpha 3 ELISA Kit. ... 35Goat Glutathione S Transferase Alpha 2 ELISA Kit. ... Goat Glutathione S Transferase Alpha 2 ELISA Kit. Product ...
Rat GSTT1 (Glutathione S Transferase Theta 1) CLIA Kit. E-CL-R0296 Regular price $650.00. $553.00 You Pay ...
  • Based on that published data on the association of prostate cancer susceptibility with polymorphisms in genes encoding Glutathione S-transferases (GSTs) were inconclusive, the aim of this study was to more precisely address the role of GSTs polymorphisms (especially, GSTT1 and GSTM1 deletions) on prostate cancer risk in Asian descent. (oncotarget.com)
  • Glutathione S-transferase polymorphisms and survival in primary malignant glioma. (cdc.gov)
  • This study examined the association between overall survival and Glutathione S-transferase Pi (GST Pi) expression and genetic polymorphism in stage C colon cancer patients after resection alone versus resection plus 5-fluourouracil-based adjuvant chemotherapy. (biomedcentral.com)
  • Polymorphism in glutathione S-transferase P1 is associated with susceptibility to chemotherapy-induced leukemia. (qxmd.com)
  • MGST1 has both glutathione transferase and peroxidase activities. (nih.gov)
  • Owing to the presence of a cysteine with a pK a value around 5 in their active site, GSTF3, F7, and F8 displayed a thiol transferase activity in addition to the usual glutathione transferase and peroxidase activities. (rcsb.org)
  • Description: A sandwich ELISA kit for detection of Glutathione S Transferase Alpha 4 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (envite.org)
  • The primary role of GSTs is to catalyze the conjugation of glutathione (GSH) with the electrophilic centers of a wide variety of molecules. (wikipedia.org)
  • There are also classes of GSTs that utilize glutathione as a cofactor rather than a substrate. (wikipedia.org)
  • In bacteria, the theta class GSTs includes all of the currently known bacterial glutathione transferases. (wikipedia.org)
  • The considerable amount of protein sequence variation has led to the general belief that GSTs carry out a very wide variety of glutathione-dependent conjugation functions. (wikipedia.org)
  • The regulation of levels of ROS, levels of oxidized and reduced glutathione and other thiols, and antioxidant enzymes (such as GSTs and glutathione reductase) are important in determination of the most stable conditions for redox control, or for activation of apoptosis. (wikipedia.org)
  • The N-terminal domain contains the glutathione-binding site and is a highly conserved region among all GSTs. (wikipedia.org)
  • The super family of glutathione S -transferases (GSTs) is composed of multiple isozymes with significant evidence of functional polymorphic variation. (nature.com)
  • Glutathione S-transferases (GSTs) detoxify potentially mutagenic and toxic DNA-reactive electrophiles, including metabolites of several chemotherapeutic agents, some of which are suspected human carcinogens. (qxmd.com)
  • In this report, we describe the glutathione transferase (GST) gene family in the dengue vector Aedes aegypti and suggest a novel role for a new class of mosquito GSTs. (lstmed.ac.uk)
  • These antioxidant enzymes are a part of the glutathione biosynthetic pathway, which is present in cyanobacteria, proteobacteria, and certain Gram-negative bacteria. (wikipedia.org)
  • Bacterial glutathione transferases of all classes are homodimeric enzymes (although heterodimeric isozymes of certain classes are also known). (wikipedia.org)
  • Glutathione level and activity of studied glutathione enzymes were determined in the supernatants. (nih.gov)
  • Genetic susceptibility to the development of chronic obstructive pulmonary disease (COPD) might depend on variation in the activities of enzymes that detoxify cigarette smoke products, such as microsomal epoxide hydrolase (mEPHX) and glutathione S-transferase (GST). (ntu.edu.tw)
  • Glutathione S-transferase P1 (GSTP1) is one of the xenobiotic-metabolizing and antioxidant enzymes, identified in the peripheral lungs. (thestemcellfoundation.com)
  • Glutathione-S-transferase also referred as GST is one of the major detoxification enzymes in parasitic helminths. (cellmolbiol.org)
  • In this study, these data have been analyzed to find all human proteins containing (or predicted to contain) the cytosolic glutathione transferase (cGST) fold. (edu.au)
  • The study aimed at identifying and purifying cytosolic glutathione transferase isoforms expressed in Pseudomonas sp. (mabjournal.com)
  • The defluorinating activity is cytosolic and has an absolute requirement for glutathione. (wgtn.ac.nz)
  • In addition to the well-characterized catalytic activity, recent evidence has shown that certain GST isozymes can regulate mitogen-activated protein kinases or can facilitate the addition of glutathione to cysteine residues in target proteins ( S -glutathionylation). (nature.com)
  • Microsomal glutathione transferase 1 (MGST1) is a member of the MAPEG family (membrane associated proteins in eicosanoid and glutathione metabolism), defined according to enzymatic activities, sequence motifs, and structural properties. (nih.gov)
  • Search at UniProt (https://www.uniprot.org/uniprot/), has indicated that there were 20 genes encoding putative glutathione transferases for the microorganism. (mabjournal.com)
  • ABSTRACT Serum levels of glutathione reductase (GR), glutathione S-transferase- (GST-) and malondialdehyde (MDA) were determined to evaluate their use in diagnosing hepatocellular damage in 75 children with liver disease. (who.int)
  • The glutathione transferase (GST) gene family is divided into 14 classes in photosynthetic organisms. (rcsb.org)
  • Analysis of the glutathione S-transferase (GST) gene family. (mabjournal.com)
  • Glutathione reductase is another enzyme that helps maintain cellular redox homeostasis by maintaining the supply of reduced glutathione. (wikipedia.org)
  • This allows positioning of several active site residues at proximity of the glutathione molecule, which itself remains unchanged in GSTF three-dimensional structures. (rcsb.org)
  • The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Protein Science : A Publication of the Protein Society, 10(11): 2176-2185. (mabjournal.com)
  • This has proven that putative GST possessed peroxidase activity and proposed to be similar to PputUW4_00801 (putative glutathione S-transferase) of Pseudomonas sp. (mabjournal.com)
  • Glutathione contains a significant amount of cysteine residues, which contributes to its nature of being readily oxidized. (wikipedia.org)
  • The -SH groups on these residues act as strong nucleophiles, which can conjugate with a variety of molecules, including other glutathione molecules. (wikipedia.org)
  • Conjugation with glutathione receptors renders toxic substances more soluble, and therefore more readily exocytosed from the cell. (wikipedia.org)
  • Additionally, the ability of seven human glutathione S-transferases (hGSTs) to catalyze the GSH conjugation of the quinoneimines formed by P450s was also investigated. (unboundmedicine.com)
  • Fluoroacetate(Compound 1080) was the only substrate tested that showed appreciable catalysed conjugation with glutathione. (wgtn.ac.nz)
  • A recent clinical study has focused on: 1- the interaction between genetic variants of glutathione S-transferases M1 and T1 (GSTM1 and GSTT1) and smoking on the risk of cardiovascular diseases, 2- the potential capacity of GSTM1 and T1 genotypes in modifying the effect of smoking on inflammation and endothelial function. (tu-dortmund.de)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Glutathione S Transferase Alpha 4 (GSTa4) in serum, plasma and other biological fluids. (envite.org)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Glutathione S Transferase Alpha 4 (GSTa4) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids. (envite.org)
  • In recent years, the importance of the endogenous plant tripeptide glutathione (GSH) has been increasingly recognized in plant-pathogen interactions due to its contribution to various signaling and defense mechanisms. (mtak.hu)
  • Glutathione S-transferase (GST) is a search Centre (NRC), Cairo, Egypt from detoxification enzyme that catalyses the 2001 to 2004, in accordance with the ethical addition of glutathione to various xeno- principles of the NRC, in collaboration with biotics [ 4 ]. (who.int)
  • The changes in reduced glutathione (GSH), activity of glutathione transferase (GST) and glutathione peroxidase (GSPx) after administration of exogenous melatonin (N-acetyl-5-methoxy-tryptamine) at a dose 20 mg/kg b.w. were investigated for five and ten days in the liver and kidney of male and female mice. (nih.gov)
  • Detection principle Glutathione S-transferase is a kind of enzyme related to liver detoxification, which is often used as an indicator of liver injury. (agtcbioproducts.com)
  • whether a decoction of Nigella sativa, Hemidesmus indicus and Smilax glabra ubhibits glutathione S-transferase (GST-P) expression in rat liver. (who.int)
  • In its reduced form, glutathione plays a key role in the regulation of reactive oxygen species (ROS) in the cell. (wikipedia.org)
  • Biophysical methods were used to elucidate the mechanism and molecular consequences of S-nitrosation of glutathione transferase (GST) P1-1, a ubiquitous homodimeric detoxification enzyme and important target for cancer therapeutics. (wits.ac.za)
  • The glutathione-requiring dehalogenating activity bound only to the GSH-BSP conjugate ligand attached to epichlorhydrin-activated Sepharose. (wgtn.ac.nz)
  • Bacterial glutathione transferases are specific to aerobic bacteria and mainly function in the detoxification of exogenous compounds and the relief of oxidative stress. (wikipedia.org)
  • Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a. (expasy.org)
  • An electron-sharing network involved in the catalytic mechanisms is functionally conserved in different glutathione transferase classes. (mabjournal.com)
  • As the key substrate in GST-mediated reactions, glutathione is one of the most conserved reducing agents in bacterial cells. (wikipedia.org)
  • Without glutathione in its reduced form, glutathione transferases are not able to utilize it as a substrate in redox reactions. (wikipedia.org)
  • The Ligandin (Non-Substrate) Binding Site of Human Pi Class Glutathione Transferase is Located in the Electrophile Binding Site (H-Site). (expasy.org)
  • Glutathione transferases play a key role in catalyzing such reactions. (wikipedia.org)
  • However, there was no difference among these transfectants neither on glutathione (GSH) level nor on c-Jun NH2-terminal kinase (JNK) activation. (thestemcellfoundation.com)
  • Melatonin caused an increase in glutathione level, the activity of glutathione peroxidase as well as glutathione transferase in the examined organs. (nih.gov)
  • The specificity of the alpha-2 helix stems from the assortment of amino acids in the domain that interacts with the glycine residue of glutathione. (wikipedia.org)
  • In addition to base assisted deprotonation of glutathione, it is proposed that a positively charged group in the GST active site assists in the leaving of the chloride ion from CDNB. (wgtn.ac.nz)
  • Glutathione may be useful for monitoring melatonin's protective role on cell damage. (nih.gov)