A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.
Porphyrins with four methyl and four propionic acid side chains attached to the pyrrole rings. Elevated levels of Coproporphyrin III in the urine and feces are major findings in patients with HEREDITARY COPROPORPHYRIA.
Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.
Iron-free derivatives of heme with 4 methyl groups, 2 hydroxyethyl groups and 2 propionic acid groups attached to the pyrrole rings. Some of these PHOTOSENSITIZING AGENTS are used in the PHOTOTHERAPY of malignant NEOPLASMS.
A diverse group of metabolic diseases characterized by errors in the biosynthetic pathway of HEME in the LIVER, the BONE MARROW, or both. They are classified by the deficiency of specific enzymes, the tissue site of enzyme defect, or the clinical features that include neurological (acute) or cutaneous (skin lesions). Porphyrias can be hereditary or acquired as a result of toxicity to the hepatic or erythropoietic marrow tissues.
Porphyrins with four acetic acid and four propionic acid side chains attached to the pyrrole rings.
Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.
Porphyrins with four methyl and two propionic acid side chains attached to the pyrrole rings.
A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.
Porphyrins with four methyl, two ethyl, and two propionic acid side chains attached to the pyrrole rings.
A sebaceous gland that, in some animals, acts as an accessory to the lacrimal gland. The harderian gland excretes fluid that facilitates movement of the third eyelid.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.
A complex mixture of monomeric and aggregated porphyrins used in the photodynamic therapy of tumors (HEMATOPORPHYRIN PHOTORADIATION). A purified component of this mixture is known as DIHEMATOPORPHYRIN ETHER.
Drugs that are pharmacologically inactive but when exposed to ultraviolet radiation or sunlight are converted to their active metabolite to produce a beneficial reaction affecting the diseased tissue. These compounds can be administered topically or systemically and have been used therapeutically to treat psoriasis and various types of neoplasms.
Therapy using oral or topical photosensitizing agents with subsequent exposure to light.
Keto acids that are derivatives of 4-oxopentanoic acids (levulinic acid).
The purified component of HEMATOPORPHYRIN DERIVATIVE, it consists of a mixture of oligomeric porphyrins. It is used in photodynamic therapy (HEMATOPORPHYRIN PHOTORADIATION); to treat malignant lesions with visible light and experimentally as an antiviral agent. It is the first drug to be approved in the use of PHOTODYNAMIC THERAPY in the United States.
Colorless reduced precursors of porphyrins in which the pyrrole rings are linked by methylene (-CH2-) bridges.
Porphobilinogen is a porphyrin precursor, specifically the organic compound intermediate in the biosynthesis of heme and chlorophyll, formed by the condensation of two pyrrole molecules in the liver and other tissues.
An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA.
An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8
Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.
An agricultural fungicide and seed treatment agent.
An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
Measurement of the intensity and quality of fluorescence.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
An autosomal dominant or acquired porphyria due to a deficiency of UROPORPHYRINOGEN DECARBOXYLASE in the LIVER. It is characterized by photosensitivity and cutaneous lesions with little or no neurologic symptoms. Type I is the acquired form and is strongly associated with liver diseases and hepatic toxicities caused by alcohol or estrogenic steroids. Type II is the familial form.
Porphyrinogens which are intermediates in heme biosynthesis. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation.
A group of metabolic diseases due to deficiency of one of a number of LIVER enzymes in the biosynthetic pathway of HEME. They are characterized by the accumulation and increased excretion of PORPHYRINS or its precursors. Clinical features include neurological symptoms (PORPHYRIA, ACUTE INTERMITTENT), cutaneous lesions due to photosensitivity (PORPHYRIA CUTANEA TARDA), or both (HEREDITARY COPROPORPHYRIA). Hepatic porphyrias can be hereditary or acquired as a result of toxicity to the hepatic tissues.
A membrane-bound flavoenzyme that catalyzes the oxygen-dependent aromatization of protoporphyrinogen IX (Protogen) to protoporphyrin IX (Proto IX). It is the last enzyme of the common branch of the HEME and CHLOROPHYLL pathways in plants, and is the molecular target of diphenyl ether-type herbicides. VARIEGATE PORPHYRIA is an autosomal dominant disorder associated with deficiency of protoporphyrinogen oxidase.
1,4-Dihydro-2,4,6-trimethyl-3,5-pyridinedicarboxylic acid diethyl ester.
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.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.
Photochemotherapy using visible light, usually red, topically or delivered locally by fiberoptic probe to tissues sensitized with hematoporphyrins.
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
Inorganic compounds that contain gold as an integral part of the molecule.
Photochemistry is the study of chemical reactions induced by absorption of light, resulting in the promotion of electrons to higher energy levels and subsequent formation of radicals or excited molecules that can undergo various reaction pathways.
A trace element that is a component of vitamin B12. It has the atomic symbol Co, atomic number 27, and atomic weight 58.93. It is used in nuclear weapons, alloys, and pigments. Deficiency in animals leads to anemia; its excess in humans can lead to erythrocytosis.
An antifungal agent used in the treatment of TINEA infections.

Do charge-remote fragmentations occur under matrix-assisted laser desorption ionization post-source decompositions and matrix-assisted laser desorption ionization collisionally activated decompositions? (1/1552)

The precursor ions of tetraphenylporphyrins that are substituted with fatty acids can be introduced into the gas phase by matrix-assisted laser desorption ionization (MALDI) and undergo post-source and collisionally activated decompositions (CAD) in a time-of-flight mass spectrometer. The goal of the research is to obtain a better understanding of post-source decompositions (PSD); specifically, we asked the question of whether ions undergoing PSD have sufficient energy to give charge-remote fragmentations along an alkyl chain. We chose the porphyrin macrocycle because we expected it to act as an inert "support," allowing the molecule to be desorbed by MALDI and to be amenable to charge-remote fragmentation. MALDI-PSD and MALDI-CAD spectra are similar to high-energy CAD spectra and considerably more informative than low-energy CAD spectra, showing that charge-remote fragmentations of the fatty acid moieties do occur upon MALDI-PSD and MALDI-CAD.  (+info)

High efficiency of benzoporphyrin derivative in the photodynamic therapy of pigmented malignant melanoma. (2/1552)

Benzoporphyrin derivative monoacid ring A (verteporfin, BPD-MA) when intravenously injected (5.5 micromol kg(-1)) to C57/BL6 mice bearing a subcutaneously transplanted B1 melanoma gave a maximal accumulation in the tumour within 1-3 h with recoveries of 1.84-1.96 micromol kg(-1). Irradiation of BPD-MA-loaded melanoma with 690-nm light from a dye laser at 3 h and 9 h post injection induced tumour necrosis and delay of tumour growth of 28 and 14 days respectively. The response of the tumour to BPD-MA photosensitization was enhanced by pretreatment with 1064-nm light from a pulse-operated Nd:YAG laser, which caused a selective breakdown of melanosomes.  (+info)

Ultrastructural changes in PAM cells after photodynamic treatment with delta-aminolevulinic acid-induced porphyrins or photosan. (3/1552)

Photodynamic therapy (PDT) is the combination of a photosensitizing drug (Ps) with light in the presence of oxygen leading to the generation of reactive molecular species and destruction of cancer cells. In this study we compared PDT with two Ps, the hematoporphyrin derivative Photosan (Ph) and delta-aminolevulinic acid (ALA)-induced endogenous protoporphyrin IX, with respect to mitochondrial function and ultrastructural alterations. The effects of PDT were investigated in PAM 212 cells after different Ps incubation times, light doses, and post-treatment periods. Both Ps induced a light dose-dependent impairment of the mitochondrial function with the dose-response curve being steep for ALA and flat for Ph. The prolongation of the incubation time from 4 to 20 h resulted in an increased reduction of mitochondrial activity after ALA PDT but not after Ph PDT. Treatment with an irradiation dose that decreased mitochondrial activity by 50% (IC50) led to early and profound changes of mitochondrial morphology in ALA photosensitized cells, whereas photosensitization with Ph resulted in more pronounced alterations of lysosomes. We conclude that at bioequivalent sublethal PDT exposures of PAM 212 cells, ALA-induced damage is primarily restricted to mitochondria, whereas Ph-induced cytotoxicity is mediated by damage of the lysosomal system.  (+info)

Five-coordinate iron-porphyrin as a model for the active site of hemoproteins. Characterization and coordination properties. (4/1552)

Preparation of iron(III)-deuteroporphyrin 6(7)-methyl ester, 7(6)-(histidine methyl ester) by coupling histidine methyl ester to deuterohemin has been performed using the mixed carboxylic/carbonic-acid-anhydride method. This compound, which is very soluble in various organic solvents, can be considered as a prosthetic group model for the active site of five-coordinate hemoproteins. In the oxidized state a basic, a neutral or an acid form can be isolated. The basic and acid forms are monomeric at all concentrations. The neutral form is found dimeric in concentrated solutions while it is monomeric at low concentration. The coordination state of iron in these various species is investigated. The neutral form reacts with ligands, such as nitrogenous organic bases, leading to six-coordinate well-known hemichromes which exhibit low-spin electron spin resonance (ESR) spectra. The reaction of anionic ligands, such as F-, CN-, NO-2 and N-3, with the neutral form model leads to unsymmetrical six-coordinate complexes whose optical and ESR spectra are similar to those of synthetic deuteromyoglobin. In benzene, toluene or dichloromethane solutions iron (II)-deuteroporphyrin 6(7)-methyl ester, 7(6)-histidine methyl ester), obtained from ferric forms by heterogeneous reduction with aqueous dithionite, exhibits an optical spectrum characteristic of a five-coordinate high-spin ferrous complex. At low temperature important spectral modifications are observed indicating a dimeric association. At room temperature it binds one nitrogenous base molecule leading to the well-known hemochrome. It reacts also with carbon monoxide with a very high affinity constant (4.5 X 10(8) M-1), comparable to that of the isolated human hemoglobin alpha and beta chains, but much higher than the values reported for other various models, suggesting that the side-chain length bearing the fifth ligand may have an important influence upon the reactivity of the sixth position of the iron ion. At low temperature in toluene or dichloromethane, this compound reversibly binds oxygen without oxidation of the iron ion while oxidation occurs at room temperature. The significance of these results is discussed in relation with the local environment, the electronic nature of the base and the immobilization of the heme group in hemoproteins.  (+info)

Reaction of the microsomal heme oxygenase with cobaltic protoporphyrin IX, and extremely poor substrate. (5/1552)

A reconstituted heme oxygenase system which was composed of a purified heme oxygenase from pig spleen microsomes and a partially purified NADPH-cytochrome c reductase from pig liver microsomes could not catalyze the conversion of cobaltic protoporphyrin IX (Co-heme) to biliverdin, although Co-heme could bind with the heme oxygenase protein to form a complex. The heme oxygenase system in the microsomes from pig spleen, rat spleen, and rat kidney also failed to oxidize Co-heme to biliverdin. Properties of the complex of Co-heme and heme oxygenase closely resembled those of cobalt myoglobin and cobalt hemoglobin; the Co-heme bound to the heme oxygenase protein did not react with cyanide and azide, the Co-heme moiety was reduced but only slowly with sodium dithionite, and the reduced form of the Co-heme did not appear to bind carbon monoxide. The co-heme bound to heme oxygenase was not reduced with the NADPH-cytochrome c reductase system in air. These findings further support the views that heme oxygenase may have a heme-binding crevice similar to those of myoglobin and hemoglobin and that reduction of heme is the prerequisite for the oxidative degradation of heme in the heme oxygenase reaction.  (+info)

Optimum porphyrin accumulation in epithelial skin tumours and psoriatic lesions after topical application of delta-aminolaevulinic acid. (6/1552)

Photodynamic therapy with topically applied delta-aminolaevulinic acid is used to treat skin tumours by employing endogenously formed porphyrins as photosensitizers. This study examines the time course of porphyrin metabolite formation after topical application of delta-aminolaevulinic acid. Porphyrin biosynthesis in human skin tumours (basal cell carcinoma, squamous cell carcinoma), in psoriatic lesions, and in normal skin was investigated. Skin areas were treated with delta-aminolaevulinic acid, and levels of total porphyrins, porphyrin metabolites and proteins were measured in samples excised after 1, 2, 4, 6, 9, 12 and 24 h. There was an increase in porphyrin biosynthesis in all tissues with maximum porphyrin levels in tumours between 2 and 6 h and in psoriatic lesions 6 h after treatment. The pattern of porphyrins showed no significant difference between normal and neoplastic skin, protoporphyrin being the predominant metabolite. The results suggest that optimum irradiation time for superficial epithelial skin tumours may be as soon as 2 h after application of delta-aminolaevulinic acid, whereas for treatment of psoriatic lesions an application time of 6 h is more suitable.  (+info)

Carbon monoxide stimulates the apical 70-pS K+ channel of the rat thick ascending limb. (7/1552)

We have investigated the expression of heme oxygenase (HO) in the rat kidney and the effects of HO-dependent heme metabolites on the apical 70-pS K+ channel in the thick ascending limb (TAL). Reverse transcriptase-PCR (RT-PCR) and Western blot analyses indicate expression of the constitutive HO form, HO-2, in the rat cortex and outer medulla. Patch-clamping showed that application of 10 microM chromium mesoporphyrin (CrMP), an inhibitor of HO, reversibly reduced the activity of the apical 70-pS K+ channel, defined by NPo, to 26% of the control value. In contrast, addition of 10 microM magnesium protoporphyrin had no significant effect on channel activity. HO involvement in regulation of the apical 70-pS K+ channel of the TAL, was further indicated by the addition of 10 microM heme-L-lysinate, which significantly stimulated the channel activity in cell-attached patches by 98%. The stimulatory effect of heme on channel activity was also observed in inside-out patches in the presence of 0.5-1 mM reduced nicotinamide adenine dinucleotide phosphate. This was completely abolished by 10 microM CrMP, suggesting that a HO-dependent metabolite of heme mediated the effect. This was further supported by exposure of the cytosolic membrane of inside-out patches to a carbon monoxide-bubbled bath solution, which increased channel activity. Moreover, carbon monoxide completely abolished the effect of 10 microM CrMP on the channel activity. In contrast, 10 microM biliverdin, another HO-dependent metabolite of heme, had no effect. We conclude that carbon monoxide produced from heme via an HO-dependent metabolic pathway stimulates the apical 70-pS K+ channel in the rat TAL.  (+info)

A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane. (8/1552)

Methylobacterium sp. strain CM4, an aerobic methylotrophic alpha-proteobacterium, is able to grow with chloromethane as a carbon and energy source. Mutants of this strain that still grew with methanol, methylamine, or formate, but were unable to grow with chloromethane, were previously obtained by miniTn5 mutagenesis. The transposon insertion sites in six of these mutants mapped to two distinct DNA fragments. The sequences of these fragments, which extended over more than 17 kb, were determined. Sequence analysis, mutant properties, and measurements of enzyme activity in cell-free extracts allowed the definition of a multistep pathway for the conversion of chloromethane to formate. The methyl group of chloromethane is first transferred by the protein CmuA (cmu: chloromethane utilization) to a corrinoid protein, from where it is transferred to H4folate by CmuB. Both CmuA and CmuB display sequence similarity to methyltransferases of methanogenic archaea. In its C-terminal part, CmuA is also very similar to corrinoid-binding proteins, indicating that it is a bifunctional protein consisting of two domains that are expressed as separate polypeptides in methyl transfer systems of methanogens. The methyl group derived from chloromethane is then processed by means of pterine-linked intermediates to formate by a pathway that appears to be distinct from those already described in Methylobacterium. Remarkable features of this pathway for the catabolism of chloromethane thus include the involvement of a corrinoid-dependent methyltransferase system for dehalogenation in an aerobe and a set of enzymes specifically involved in funneling the C1 moiety derived from chloromethane into central metabolism.  (+info)

Porphyrins are complex organic compounds that contain four pyrrole rings joined together by methine bridges (=CH-). They play a crucial role in the biochemistry of many organisms, as they form the core structure of various heme proteins and other metalloproteins. Some examples of these proteins include hemoglobin, myoglobin, cytochromes, and catalases, which are involved in essential processes such as oxygen transport, electron transfer, and oxidative metabolism.

In the human body, porphyrins are synthesized through a series of enzymatic reactions known as the heme biosynthesis pathway. Disruptions in this pathway can lead to an accumulation of porphyrins or their precursors, resulting in various medical conditions called porphyrias. These disorders can manifest as neurological symptoms, skin lesions, and gastrointestinal issues, depending on the specific type of porphyria and the site of enzyme deficiency.

It is important to note that while porphyrins are essential for life, their accumulation in excessive amounts or at inappropriate locations can result in pathological conditions. Therefore, understanding the regulation and function of porphyrin metabolism is crucial for diagnosing and managing porphyrias and other related disorders.

Coproporphyrins are porphyrin molecules that contain four carboxylic acid groups (four propionic side chains and two acetic side chains). They are intermediates in the biosynthesis of heme, which is a component of hemoglobin and other hemoproteins. Coproporphyrins can be further metabolized to form protoporphyrins, which are converted into heme by the enzyme ferrochelatase.

Coproporphyrins can be excreted in urine and feces, and their levels can be measured in clinical testing. Elevated coproporphyrin levels in urine or feces may indicate the presence of certain medical conditions, such as lead poisoning, porphyrias, or liver dysfunction.

There are two types of coproporphyrins, coproporphyrin I and coproporphyrin III, which differ in the arrangement of their side chains. Coproporphyrin III is the form that is normally produced in the body, while coproporphyrin I is a byproduct of abnormal porphyrin metabolism.

Metalloporphyrins are a type of porphyrin molecule that contain a metal ion at their center. Porphyrins are complex organic compounds containing four modified pyrrole rings connected to form a planar, aromatic ring known as a porphine. When a metal ion is incorporated into the center of the porphyrin ring, it forms a metalloporphyrin.

These molecules have great biological significance, as they are involved in various essential processes within living organisms. For instance, heme, a type of iron-containing porphyrin, plays a crucial role in oxygen transport and storage in the body by forming part of hemoglobin and myoglobin molecules. Chlorophyll, another metalloporphyrin with magnesium at its center, is essential for photosynthesis in plants, algae, and some bacteria.

Metalloporphyrins have also found applications in several industrial and medical fields, including catalysis, sensors, and pharmaceuticals. Their unique structure and properties make them valuable tools for researchers and scientists to study and utilize in various ways.

Hematoporphyrins are porphyrin derivatives that contain iron and are found in hemoglobin, the oxygen-carrying protein in red blood cells. Specifically, hematoporphyrin is a complex organic compound with the chemical formula C34H32N4O4Fe. It is a reddish-brown powder that is soluble in alcohol and ether but insoluble in water.

Hematoporphyrins have been studied for their potential use in photodynamic therapy, which involves using light to activate a photosensitizing agent like hematoporphyrin to destroy cancer cells. However, other porphyrin derivatives such as Photofrin are more commonly used in clinical practice due to their superior properties and safety profile.

Porphyrias are a group of rare genetic disorders that affect the production of heme, a component in hemoglobin that carries oxygen in the blood. The diseases are caused by mutations in the genes involved in the production of heme, leading to the buildup of porphyrins or their precursors in the body. These substances can be toxic and can cause various symptoms depending on the specific type of porphyria. Symptoms may include abdominal pain, neurological problems, and skin issues. Porphyrias are typically divided into two categories: acute porphyrias, which affect the nervous system, and cutaneous porphyrias, which primarily affect the skin.

Uroporphyrins are porphyrin derivatives that contain four carboxylic acid groups. They are intermediates in the biosynthesis of heme, which is a component of hemoglobin and other hemoproteins. Uroporphyrinogen I and III are precursors to uroporphyrin I and III, respectively, through the action of uroporphyrinogen decarboxylase.

Uroporphyrin I and III differ in the position of acetate and propionate side chains on the porphyrin ring. Uroporphyrins are usually elevated in the urine of patients with certain inherited metabolic disorders, such as acute intermittent porphyria, variegate porphyria, and hereditary coproporphyria, due to enzyme deficiencies in the heme biosynthetic pathway.

The measurement of uroporphyrins in urine or other body fluids can be helpful in diagnosing and monitoring these disorders.

Protoporphyrins are organic compounds that are the immediate precursors to heme in the porphyrin synthesis pathway. They are composed of a porphyrin ring, which is a large, complex ring made up of four pyrrole rings joined together, with an acetate and a propionate side chain at each pyrrole. Protoporphyrins are commonly found in nature and are important components of many biological systems, including hemoglobin, the protein in red blood cells that carries oxygen throughout the body.

There are several different types of protoporphyrins, including protoporphyrin IX, which is the most common form found in humans and other animals. Protoporphyrins can be measured in the blood or other tissues as a way to diagnose or monitor certain medical conditions, such as lead poisoning or porphyrias, which are rare genetic disorders that affect the production of heme. Elevated levels of protoporphyrins in the blood or tissues can indicate the presence of these conditions and may require further evaluation and treatment.

Deuteroporphyrins are porphyrin derivatives that contain two carboxylic acid side chains. They are intermediates in the biosynthesis of heme and chlorophyll, which are essential molecules for biological processes such as oxygen transport and photosynthesis, respectively.

Deuteroporphyrins can be further classified into isomers based on the position of the carboxylic acid side chains. The most common isomer is deuteroporphyrin IX, which has the carboxylic acid side chains located at positions 1 and 2 relative to the pyrrole nitrogen atoms.

Deuteroporphyrins have been studied in various medical contexts, including as potential markers of porphyria, a group of metabolic disorders characterized by the accumulation of porphyrin precursors. Additionally, deuteroporphyrins and their derivatives have been investigated for their potential use in photodynamic therapy, a treatment modality that uses light-activated drugs to destroy cancer cells.

Aminolevulinic acid (ALA) is a naturally occurring compound in the human body and is a key precursor in the biosynthesis of heme, which is a component of hemoglobin in red blood cells. It is also used as a photosensitizer in dermatology for the treatment of certain types of skin conditions such as actinic keratosis and basal cell carcinoma.

In medical terms, ALA is classified as an α-keto acid and a porphyrin precursor. It is synthesized in the mitochondria from glycine and succinyl-CoA in a reaction catalyzed by the enzyme aminolevulinic acid synthase. After its synthesis, ALA is transported to the cytosol where it undergoes further metabolism to form porphyrins, which are then used for heme biosynthesis in the mitochondria.

In dermatology, topical application of ALA followed by exposure to a specific wavelength of light can lead to the production of reactive oxygen species that destroy abnormal cells in the skin while leaving healthy cells unharmed. This makes it an effective treatment for precancerous and cancerous lesions on the skin.

It is important to note that ALA can cause photosensitivity, which means that patients who have undergone ALA-based treatments should avoid exposure to sunlight or other sources of bright light for a period of time after the treatment to prevent adverse reactions.

Mesoporphyrins are a type of porphyrin, which are organic compounds containing four pyrrole rings connected by methine bridges in a cyclic arrangement. Porphyrins are important components of various biological molecules such as hemoglobin, myoglobin, and cytochromes.

Mesoporphyrins have a specific structure with two propionic acid side chains and two acetic acid side chains attached to the pyrrole rings. They are intermediates in the biosynthesis of heme, which is a complex formed by the insertion of iron into protoporphyrin IX, a type of porphyrin.

Mesoporphyrins have been used in medical research and clinical settings as photosensitizers for photodynamic therapy (PDT), a treatment that uses light to activate a photosensitizing agent to destroy abnormal cells or tissues. In particular, mesoporphyrin IX has been used for the PDT treatment of various types of cancer, such as bladder, esophageal, and lung cancer, as well as for the treatment of age-related macular degeneration (AMD), a leading cause of vision loss in older adults.

It is important to note that mesoporphyrins are not typically used as a diagnostic tool or a therapeutic agent in routine clinical practice, but rather as part of experimental research and clinical trials.

The Harderian gland is a specialized exocrine gland located in many vertebrate species, including birds and mammals. In humans, it is rudimentary and not fully developed. However, in other animals like rodents, lagomorphs (rabbits and hares), and some reptiles, this gland plays a significant role.

The Harderian gland is primarily responsible for producing and secreting lipids, which help to lubricate the eye's surface and the nictitating membrane (third eyelid). This lubrication ensures that the eyes remain moist and protected from dryness and external irritants. Additionally, the secretions of the Harderian gland contain immunoglobulins, which contribute to the animal's immune defense system by providing protection against pathogens.

In some animals, the Harderian gland also has a role in pheromone production and communication. The study and understanding of this gland are particularly important in toxicological research, as it is often used as an indicator of environmental pollutant exposure and their effects on wildlife.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

Ferrochelatase is a medical/biochemical term that refers to an enzyme called Fe-chelatase or heme synthase. This enzyme plays a crucial role in the biosynthesis of heme, which is a vital component of hemoglobin, cytochromes, and other important biological molecules.

Ferrochelatase functions by catalyzing the insertion of ferrous iron (Fe2+) into protoporphyrin IX, the final step in heme biosynthesis. This enzyme is located within the inner mitochondrial membrane of cells and is widely expressed in various tissues, with particularly high levels found in erythroid precursor cells, liver, and brain.

Defects or mutations in the ferrochelatase gene can lead to a rare genetic disorder called erythropoietic protoporphyria (EPP), which is characterized by an accumulation of protoporphyrin IX in red blood cells, plasma, and other tissues. This accumulation results in photosensitivity, skin lesions, and potential complications such as liver dysfunction and gallstones.

Hematoporphyrin derivative (HPD) is not a medical term per se, but rather a historical term used in the field of oncology to describe a mixture of porphyrin derivatives. HPD was initially developed as a photosensitizer for photodynamic therapy (PDT), a type of cancer treatment that uses light to activate a chemical, which then reacts with oxygen to kill nearby cells.

HPD is derived from hematoporphyrin, a naturally occurring porphyrin found in small amounts in blood. The derivative is created through a series of chemical reactions that result in a mixture of monomeric and dimeric porphyrins. These compounds have the ability to accumulate in cancer cells, making them more sensitive to light-induced damage during PDT.

Although HPD was an important early photosensitizer in the development of PDT, it has largely been replaced by more efficient and specific agents, such as Photofrin and temoporfin. Nonetheless, the concept and principles behind HPD's use in PDT remain relevant to the ongoing research and clinical application of this promising cancer treatment modality.

Photosensitizing agents are substances that, when exposed to light, particularly ultraviolet or visible light, can cause chemical reactions leading to the production of reactive oxygen species. These reactive oxygen species can interact with biological tissues, leading to damage and a variety of phototoxic or photoallergic adverse effects.

Photosensitizing agents are used in various medical fields, including dermatology and oncology. In dermatology, they are often used in the treatment of conditions such as psoriasis and eczema, where a photosensitizer is applied to the skin and then activated with light to reduce inflammation and slow the growth of skin cells.

In oncology, photosensitizing agents are used in photodynamic therapy (PDT), a type of cancer treatment that involves administering a photosensitizer, allowing it to accumulate in cancer cells, and then exposing the area to light. The light activates the photosensitizer, which produces reactive oxygen species that damage the cancer cells, leading to their death.

Examples of photosensitizing agents include porphyrins, chlorophyll derivatives, and certain antibiotics such as tetracyclines and fluoroquinolones. It is important for healthcare providers to be aware of the potential for photosensitivity when prescribing these medications and to inform patients of the risks associated with exposure to light.

Photochemotherapy is a medical treatment that combines the use of drugs and light to treat various skin conditions. The most common type of photochemotherapy is PUVA (Psoralen + UVA), where the patient takes a photosensitizing medication called psoralen, followed by exposure to ultraviolet A (UVA) light.

The psoralen makes the skin more sensitive to the UVA light, which helps to reduce inflammation and suppress the overactive immune response that contributes to many skin conditions. This therapy is often used to treat severe cases of psoriasis, eczema, and mycosis fungoides (a type of cutaneous T-cell lymphoma). It's important to note that photochemotherapy can increase the risk of skin cancer and cataracts, so it should only be administered under the close supervision of a healthcare professional.

Levulinic acid is not specifically a medical term, but it is a chemical compound with the formula C5H8O2. It is a white crystalline solid that is used in the production of various chemicals and materials. However, I can provide you with some general information about levulinic acid:

Levulinic acid is a saturated carboxylic acid, which means it contains a carboxyl group (-COOH) and is fully saturated with hydrogen atoms. It is an alpha-beta unsaturated carboxylic acid due to the presence of a carbon-carbon double bond (C=C) between the second and third carbon atoms in its structure.

Levulinic acid can be found naturally in small amounts in various fruits, such as apples and grapes, and is also present in some fermented foods like beer and wine. It can be produced industrially from biomass sources, such as cellulose or lignocellulosic materials, through a process called acid hydrolysis.

In the medical field, levulinic acid may have potential applications as an antimicrobial agent due to its ability to inhibit the growth of certain bacteria and fungi. It is also used in the synthesis of pharmaceuticals and other chemical products. However, it is not a substance that is typically directly associated with medical treatment or diagnosis.

Dihematoporphyrin ether (DHE) is a photosensitizing agent used in photodynamic therapy for the treatment of various types of cancer. It is a porphyrin derivative that is selectively taken up by cancer cells, and when activated by light of a specific wavelength, it produces singlet oxygen and other reactive oxygen species that can destroy the cancer cells.

DHE is typically administered intravenously and then followed by exposure to laser light at a wavelength of 652 nm. The therapy has been used to treat various types of cancer including skin, lung, bladder, and brain tumors. However, it should be noted that the use of DHE and other photosensitizing agents in photodynamic therapy is still considered experimental and further research is needed to establish its safety and efficacy.

Porphyrinogens are organic compounds that are the precursors to porphyrins, which are ring-shaped molecules found in many important biological molecules such as hemoglobin and cytochromes. Porphyrinogens are themselves derived from the condensation of four pyrrole molecules, and they undergo further reactions to form porphyrins.

In particular, porphyrinogens are intermediates in the biosynthesis of heme, which is a complex organic ring-shaped molecule that contains iron and plays a critical role in oxygen transport and storage in the body. Abnormalities in heme biosynthesis can lead to various medical conditions known as porphyrias, which are characterized by the accumulation of porphyrinogens and other intermediates in this pathway. These conditions can cause a range of symptoms, including neurological problems, skin sensitivity to light, and abdominal pain.

Porphobilinogen (PBG) is a bioactive compound that plays a crucial role in the biosynthesis pathway of heme, which is an essential component of hemoglobin and other hemoproteins. It is a porphyrin precursor and is synthesized from aminolevulinic acid (ALA) by the enzyme ALA dehydratase in the second step of heme biosynthesis.

In medical terms, abnormal accumulation or increased levels of PBG in the body can indicate an underlying disorder in heme biosynthesis, such as acute intermittent porphyria (AIP), variegate porphyria (VP), or hereditary coproporphyria (HCP). These disorders are known as porphyrias and are characterized by the buildup of porphyrin precursors in various tissues, leading to neurological and gastrointestinal symptoms.

Therefore, measuring PBG levels in urine or blood can help diagnose and monitor these conditions.

Uroporphyrinogen decarboxylase is a vital enzyme in the biosynthetic pathway of heme, which is a crucial component of hemoglobin in red blood cells. This enzyme is responsible for catalyzing the decarboxylation of uroporphyrinogen III, a colorless porphyrinogen, to produce coproporphyrinogen III, a brownish-red porphyrinogen.

The reaction involves the sequential removal of four carboxyl groups from the four acetic acid side chains of uroporphyrinogen III, resulting in the formation of coproporphyrinogen III. This enzyme's activity is critical for the normal biosynthesis of heme, and any defects or deficiencies in its function can lead to various porphyrias, a group of metabolic disorders characterized by the accumulation of porphyrins and their precursors in the body.

The gene responsible for encoding uroporphyrinogen decarboxylase is UROD, located on chromosome 1p34.1. Mutations in this gene can lead to a deficiency in the enzyme's activity, causing an autosomal recessive disorder known as congenital erythropoietic porphyria (CEP), also referred to as Günther's disease. This condition is characterized by severe photosensitivity, hemolytic anemia, and scarring or thickening of the skin.

Hydroxymethylbilane Synthase (HMBS) is an enzyme that plays a crucial role in the metabolic pathway known as heme biosynthesis. Heme is an essential component of various proteins, including hemoglobin, which is responsible for oxygen transport in the blood.

The HMBS enzyme catalyzes the conversion of aminolevulinic acid (ALA) and glycine into a linear tetrapyrrole intermediate called hydroxymethylbilane. This reaction is the third step in the heme biosynthesis pathway, and it takes place in the mitochondria of cells.

Deficiencies in HMBS can lead to a rare genetic disorder called acute intermittent porphyria (AIP), which is characterized by neurovisceral attacks and neurological symptoms such as abdominal pain, vomiting, hypertension, tachycardia, and mental disturbances.

Hemin is defined as the iron(III) complex of protoporphyrin IX, which is a porphyrin derivative. It is a naturally occurring substance that is involved in various biological processes, most notably in the form of heme, which is a component of hemoglobin and other hemoproteins. Hemin is also used in medical research and therapy, such as in the treatment of methemoglobinemia and lead poisoning.

Hexachlorobenzene (HCB) is not typically included in standard medical textbooks or resources as it's more of a environmental and industrial chemical. However, I can provide you with an definition from a toxicological perspective:

Hexachlorobenzene (C6Cl6) is an organic compound that consists of a benzene ring with six chlorine atoms attached to it. It is a persistent organic pollutant, which means it does not break down easily and can accumulate in the environment and living organisms. HCB has been used as a pesticide, fungicide, and chemical intermediate in various industrial processes. Exposure to this compound can lead to several health issues, including skin lesions, damage to the nervous system, and impaired immune function. It's also considered a possible human carcinogen by some agencies. Long-term environmental exposure to HCB is of particular concern due to its bioaccumulation in the food chain and potential adverse effects on human health and the environment.

5-Aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, a metabolic pathway that produces heme, a porphyrin ring with an iron atom at its center. Heme is a crucial component of hemoglobin, cytochromes, and other important molecules in the body.

ALAS exists in two forms: ALAS1 and ALAS2. ALAS1 is expressed in all tissues, while ALAS2 is primarily expressed in erythroid cells (precursors to red blood cells). The reaction catalyzed by ALAS involves the condensation of glycine and succinyl-CoA to form 5-aminolevulinate.

Deficiencies or mutations in the ALAS2 gene can lead to a rare genetic disorder called X-linked sideroblastic anemia, which is characterized by abnormal red blood cell maturation and iron overload in mitochondria.

Heme proteins are a type of protein that contain a heme group, which is a prosthetic group composed of an iron atom contained in the center of a large organic ring called a porphyrin. The heme group gives these proteins their characteristic red color. Hemeproteins have various important functions in biological systems, including oxygen transport (e.g., hemoglobin), electron transfer (e.g., cytochromes), and enzymatic catalysis (e.g., peroxidases and catalases). The heme group can bind and release gases, such as oxygen and carbon monoxide, and can participate in redox reactions due to the ease with which iron can change its oxidation state.

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.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Porphyria Cutanea Tarda (PCT) is a type of porphyria, a group of rare genetic disorders that affect the production of heme, a component in hemoglobin. PCT is primarily an acquired disorder, although it can have a hereditary component as well.

In PCT, there is a dysfunction in the enzyme uroporphyrinogen decarboxylase (UROD), which leads to the accumulation of porphyrins and porphyrin precursors in the skin. This buildup causes the characteristic symptoms of PCT, which include:

* Blisters, particularly on sun-exposed areas such as the hands and face
* Fragile, thin skin that tears easily
* Scarring
* Hypertrichosis (abnormal hair growth)
* Changes in skin color, including redness, increased pigmentation, or loss of pigment

PCT is typically triggered by factors such as alcohol consumption, estrogen use, hepatitis C infection, and exposure to certain chemicals. Treatment often involves addressing these triggers, along with the use of phlebotomy (removal of blood) or low-dose hydroxychloroquine to reduce porphyrin levels in the body.

It's important to note that PCT is a complex disorder and its diagnosis and management should be done by healthcare professionals with experience in managing porphyrias.

Uroporphyrinogens are organic compounds that are intermediate products in the synthesis of heme, which is a crucial component of hemoglobin and other important molecules in the body. Specifically, uroporphyrinogens are tetrapyrroles, which means they contain four pyrrole rings linked together. They have eight carboxylic acid side chains and two propionic acid side chains.

There are two types of uroporphyrinogens: Type I and Type III. Uroporphyrinogen III is the precursor to heme, while uroporphyrinogen I is a dead-end metabolite that is not used in heme synthesis. Defects in the enzymes involved in heme biosynthesis can lead to various porphyrias, which are genetic disorders characterized by the accumulation of porphyrins and their precursors in the body.

Hepatic porphyrias are a group of rare genetic disorders that affect the production of heme in the liver. Heme is a crucial component of hemoglobin, the protein in red blood cells that carries oxygen throughout the body. In hepatic porphyrias, there is a buildup of porphyrins or porphyrin precursors, which are toxic and can cause a variety of symptoms.

The four types of hepatic porphyrias are:

1. Acute Intermittent Porphyria (AIP): This is the most common type of hepatic porphyria. It is characterized by attacks of abdominal pain, nausea, vomiting, constipation, and neurological symptoms such as muscle weakness, seizures, and mental changes.
2. Variegate Porphyria (VP): This type of porphyria is more common in South Africa but can occur worldwide. It is characterized by skin symptoms such as blistering and scarring after exposure to sunlight, as well as acute attacks similar to those seen in AIP.
3. Hereditary Coproporphyria (HCP): This type of porphyria is similar to VP, but the symptoms are usually less severe. It can cause both skin symptoms and acute attacks.
4. ALA Dehydratase Deficiency Porphyria (ADDP): This is the rarest type of hepatic porphyria. It is characterized by severe neurological symptoms and is often diagnosed in infancy or early childhood.

The diagnosis of hepatic porphyrias typically involves measuring the levels of porphyrins and their precursors in the urine, blood, or stool during an attack or between attacks. Treatment may include avoiding trigger factors such as certain medications, alcohol, and smoking, as well as providing supportive care during acute attacks. In some cases, medication to reduce porphyrin production or prevent attacks may be necessary.

Protoporphyrinogen Oxidase (PPO) is a mitochondrial enzyme that plays a crucial role in the heme biosynthesis pathway. It catalyzes the oxidation of protoporphyrinogen IX to protporphyrin IX, which is the penultimate step in the production of heme. This enzyme is the target of certain herbicides, such as those containing the active ingredient diphenyl ether, and genetic deficiencies in PPO can lead to a rare genetic disorder called Protoporphyria.

I apologize, but I am unable to find a medical definition for "dicarbethoxydihydrocollidine." It is possible that this term does not have a specific meaning within the field of medicine. A more general search indicates that dicarbethoxydihydrocollidine may be a chemical compound used in research or industry, but it does not appear to have direct relevance to medical diagnosis, treatment, or health. If you have further questions or need information on a related medical topic, I would be happy to help you with those.

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.

In the context of medicine, iron is an essential micromineral and key component of various proteins and enzymes. It plays a crucial role in oxygen transport, DNA synthesis, and energy production within the body. Iron exists in two main forms: heme and non-heme. Heme iron is derived from hemoglobin and myoglobin in animal products, while non-heme iron comes from plant sources and supplements.

The recommended daily allowance (RDA) for iron varies depending on age, sex, and life stage:

* For men aged 19-50 years, the RDA is 8 mg/day
* For women aged 19-50 years, the RDA is 18 mg/day
* During pregnancy, the RDA increases to 27 mg/day
* During lactation, the RDA for breastfeeding mothers is 9 mg/day

Iron deficiency can lead to anemia, characterized by fatigue, weakness, and shortness of breath. Excessive iron intake may result in iron overload, causing damage to organs such as the liver and heart. Balanced iron levels are essential for maintaining optimal health.

Porphobilinogen Synthase (also known as PBGD or hydroxymethylbilane synthase) is an enzyme that catalyzes the second step in the heme biosynthesis pathway. This enzyme is responsible for converting two molecules of porphobilinogen into a linear tetrapyrrole called hydroxymethylbilane, which is then converted into uroporphyrinogen III by uroporphyrinogen III synthase.

Deficiency in Porphobilinogen Synthase can lead to a rare genetic disorder known as acute intermittent porphyria (AIP), which is characterized by the accumulation of porphobilinogen and other precursors in the heme biosynthesis pathway, resulting in neurovisceral symptoms such as abdominal pain, vomiting, neuropathy, and psychiatric disturbances.

Hematoporphyrin photoradiation is not a widely recognized medical term, but I believe you may be referring to "PhotoDynamic Therapy (PDT) using Hematoporphyrin Derivative (HpD)." Here's the definition:

PhotoDynamic Therapy (PDT) using Hematoporphyrin Derivative (HpD) is a medical procedure that involves the use of a photosensitizing agent, such as Hematoporphyrin Derivative (HpD), and light to treat various types of cancer and other diseases. The process begins with the administration of the photosensitizer, which accumulates in malignant cells more than in normal cells. After some time, the treatment site is exposed to a specific wavelength of light that activates the photosensitizer, causing it to produce a form of oxygen that kills the cancerous cells. This procedure can be used alone or in combination with other therapies for treating various types of cancer, such as skin, lung, and bladder cancer.

Myoglobin is a protein found in the muscle tissue, particularly in red or skeletal muscles. It belongs to the globin family and has a similar structure to hemoglobin, another oxygen-binding protein found in red blood cells. Myoglobin's primary function is to store oxygen within the muscle cells, making it readily available for use during periods of increased oxygen demand, such as during physical exertion.

Myoglobin contains heme groups that bind to and release oxygen molecules. The protein has a higher affinity for oxygen than hemoglobin, allowing it to maintain its bound oxygen even in low-oxygen environments. When muscle cells are damaged or undergo necrosis (cell death), myoglobin is released into the bloodstream and can be detected in serum or urine samples. Elevated levels of myoglobin in the blood or urine may indicate muscle injury, trauma, or diseases affecting muscle integrity, such as rhabdomyolysis or muscular dystrophies.

Gold compounds refer to chemical combinations in which gold atoms are bonded with other elements. In the context of medicine, particularly in the field of rheumatology, gold compounds have been used as disease-modifying antirheumatic drugs (DMARDs) for the treatment of conditions such as rheumatoid arthritis.

The most commonly used gold compound is auranofin, which contains gold in the +1 oxidation state. Auranofin is an oral medication that can help reduce inflammation and slow down joint damage caused by rheumatoid arthritis. It works by inhibiting certain enzymes involved in the inflammatory response.

Other gold compounds, such as sodium aurothiomalate and gold thioglucose, are administered parenterally (usually intramuscularly) and contain gold in the +3 oxidation state. These medications also have anti-inflammatory properties and can help alleviate symptoms of rheumatoid arthritis.

It is important to note that the use of gold compounds as a treatment for rheumatoid arthritis has declined over time due to their side effects, which may include kidney damage, skin reactions, mouth ulcers, and bone marrow suppression. They are generally reserved for patients who have not responded well to other DMARDs or biologic agents.

I'm sorry for any confusion, but "photochemistry" is not a term typically used in medical definitions. Photochemistry is a branch of chemistry that deals with the chemical effects of light. It involves the absorption of light by a substance, which can lead to the promotion of an electron to a higher energy state, and subsequently result in various chemical reactions.

In a medical context, photochemical processes might be discussed in relation to certain therapies or diagnostic techniques, such as photodynamic therapy for cancer treatment, where a photosensitizing agent is used that reacts with light to produce singlet oxygen or other reactive species to destroy nearby cells. However, it's not a term used to define a specific medical condition or concept in the same way that one might define "inflammation" or "metabolism."

Cobalt is a chemical element with the symbol Co and atomic number 27. It is a hard, silver-white, lustrous, and brittle metal that is found naturally only in chemically combined form, except for small amounts found in meteorites. Cobalt is used primarily in the production of magnetic, wear-resistant, and high-strength alloys, as well as in the manufacture of batteries, magnets, and pigments.

In a medical context, cobalt is sometimes used in the form of cobalt-60, a radioactive isotope, for cancer treatment through radiation therapy. Cobalt-60 emits gamma rays that can be directed at tumors to destroy cancer cells. Additionally, small amounts of cobalt are present in some vitamin B12 supplements and fortified foods, as cobalt is an essential component of vitamin B12. However, exposure to high levels of cobalt can be harmful and may cause health effects such as allergic reactions, lung damage, heart problems, and neurological issues.

Griseofulvin is an antifungal medication used to treat various fungal infections, including those affecting the skin, hair, and nails. It works by inhibiting the growth of fungi, particularly dermatophytes, which cause these infections. Griseofulvin can be obtained through a prescription and is available in oral (by mouth) and topical (on the skin) forms.

The primary mechanism of action for griseofulvin involves binding to tubulin, a protein necessary for fungal cell division. This interaction disrupts the formation of microtubules, which are crucial for the fungal cell's structural integrity and growth. As a result, the fungi cannot grow and multiply, allowing the infected tissue to heal and the infection to resolve.

Common side effects associated with griseofulvin use include gastrointestinal symptoms (e.g., nausea, vomiting, diarrhea), headache, dizziness, and skin rashes. It is essential to follow the prescribing physician's instructions carefully when taking griseofulvin, as improper usage may lead to reduced effectiveness or increased risk of side effects.

It is important to note that griseofulvin has limited use in modern medicine due to the development of newer and more effective antifungal agents. However, it remains a valuable option for specific fungal infections, particularly those resistant to other treatments.

The Boron porphyrin compounds can be synthesized either from the free base porphyrin or from a lithium porphyrin complex as ... This suggests the porphyrin pocket is more likely to accommodate two boron atoms rather than one. Indeed, each boron porphyrin ... Boron porphyrins are of interest because of the unique geometric environment to which both boron and porphyrin are subjected ... Boron porphyrins are a variety of porphyrin, a common macrocycle used for photosensitization and metal trapping applications, ...
The porphyrin complex in each of these plasma samples had a fluorescence emission maximum at 626 +/- 1 nm. Twelve patients with ... Ten patients with variegate porphyria were uniformly found to have distinctive plasma porphyrin fluorescence wavelength maxima ... A plasma porphyrin fluorescence marker for variegate porphyria Arch Dermatol. 1980 May;116(5):543-7. ... The porphyrin complex in each of these plasma samples had a fluorescence emission maximum at 626 +/- 1 nm. Twelve patients with ...
Porphyrin tests measure the level of porphyrin in your blood, urine, or stool. Its used to diagnose a rare group of disorders ... What are porphyrin tests?. Porphyrin tests measure the level of porphyrins in your blood, urine (pee), or stool (poop). Your ... What happens during porphyrin testing?. Porphyrins can be tested in blood, urine, or stool. The most common types of porphyrin ... Why do I need a porphyrin test?. You may need a porphyrin test if you have symptoms of porphyria. Each porphyria group has ...
Solar Urticaria and Disturbed Metabolism of Porphyrins Subject Area: Dermatology , Immunology and Allergy ... R.C. Beljaards, D.P. Bruynzeel; Solar Urticaria and Disturbed Metabolism of Porphyrins. Dermatologica 1 April 1991; 182 (4): ...
Plasma porphyrin levels were determined in a group of 50 workers exposed to lead. The mean value obtained (0·7 μg./100 ml.) was ... no correlation was found between plasma porphyrin levels and urinary porphyrin levels. ... Chromatography of the plasma porphyrins from lead workers showed that some protoporphyrin was present in addition to the ... found to be higher than that obtained from a control group (0·2 μg./100 ml.). Although urinary porphyrin levels in the lead ...
Carbazole-Containing Expanded Porphyrins. Author: ChemistryViews. Porphyrins are macrocyclic organic compounds, containing four ... Expanded porphyrins-larger analogues of these compounds-can be interesting, e.g., for their electronic and optical properties ... According to the team, it is the first example of a BODIPY-type expanded porphyrin to show solid-state lasing. ... and colleagues have synthesized two carbazole-containing expanded porphyrins (pictured), called octaphyrins, as well as the bis ...
Self-assembly of a strapped linear porphyrin oligomer on HOPG  Bellamy-Carter, Abigail; Saywell, Alex (The University of ... Van der Waals-induced chromatic shifts in hydrogen-bonded two-dimensional porphyrin arrays on boron nitride  Beton, Peter ( ... Ordering, flexibility and frustration in arrays of porphyrin nanorings  Beton, Peter (The University of Nottingham, 2020-04-01 ... Organisation and ordering of 1D porphyrin polymers synthesised by on-surface Glaser coupling  Saywell, Alex (The University of ...
Ni-Cu ion exchange observed for Ni(II)-porphyrins on Cu(111) C. M. Doyle, J. P. Cunniffe, S. A. Krasnikov, A. B. Preobrajenski ... Ni-Cu ion exchange observed for Ni(ii)-porphyrins on Cu(111)† ...
Combined Therapy For Squamous Carcinoma Cells: Application of Porphyrin-Alkaloid Modified Gold Nanoparticles. Written By ...
Iron porphyrin catalysed light driven C-H bond amination and alkene aziridination with organic azides Y. Du, C. Zhou, W. To, H ... Iron porphyrin catalysed light driven C-H bond amination and alkene aziridination with organic azides† ... Herein is described an iron(III) porphyrin catalysed sp3 C-H amination and alkene aziridination with selectivity by using ... Mechanistic studies revealed that iron porphyrin plays a dual role as a photosensitizer and as a catalyst giving rise to a ...
HomePublicationsAxial ligand modified high valent tin (IV) porphyrins: synthesis, structure, photophysical studies and ... Axial ligand modified high valent tin (IV) porphyrins: synthesis, structure, photophysical studies and photodynamic ...
The porphyrin content was higher in pork meat than in turkey meat. It increased during storage time when the meat was packed in ... Measurement of lipid oxidation and porphyrins in high oxygen modified atmosphere and vacuum-packed minced turkey and pork meat ... Measurement of lipid oxidation and porphyrins in high oxygen modified atmosphere and vacuum-packed minced turkey and pork meat ... Measurement of lipid oxidation and porphyrins in high oxygen modified atmosphere and vacuum-packed minced turkey and pork meat ...
Manganese porphyrins have been extensively investigated as model systems for the natural enzyme cytochrome P450 and as ... Here, we report single-molecule studies of the multistep reaction of manganese porphyrins with molecular oxygen at a solid/ ... Detection of different oxidation states of individual manganese porphyrins during their reaction with oxygen at a solid/liquid ...
To systematically explore the effect of quantum interferences, we designed and synthesized two new classes of porphyrins, P1 ... To systematically explore the effect of quantum interferences, we designed and synthesized two new classes of porphyrins, P1 ... To systematically explore the effect of quantum interferences, we designed and synthesized two new classes of porphyrins, P1 ... Electrical Conductance and Thermopower of β-Substituted Porphyrin Molecular Junctions─Synthesis and Transport. *Mark ...
Bioanalysis Using Porphyrin Derivatives. Enzymes hydrolyzing water-soluble short-chain triacylglycerols to corresponding fatty ... using sodium salt of tetra sulfonatophenyl porphyrin (Na-TSPP) as a chromogenic indicator that can also overcome the problem of ...
Porphyrins. *Rashmirekha Satapathy, Barada Prasanna Dash, John A. Maguire* and Narayan S. Hosmane*. New developments in the ... Electrooxidation and determination of sulfite in ethanol-water solutions using poly-Cu(II)-tetrakis(x-aminophenyl)porphyrin/ ... The DNA-Porphyrin Interactions Studied by Vibrational and Electronic Circular Dichroism Spectroscopy. 2005, Vol. 70, Issue 11, ... Synthesis of Porphyrin Receptors Modified by Glycosylated Steroids. 2004, Vol. 69, Issue 5, pp. 1149-1160 [Abstract] ...
Novel concepts for type II photooxygenation and type B photocatalysis: Chiral porphyrins, Pluronic environment and nanosized ... Novel concepts for type II photooxygenation and type B photocatalysis: Chiral porphyrins, Pluronic environment and nanosized ... Novel concepts for type II photooxygenation and type B photocatalysis: Chiral porphyrins, Pluronic environment and nanosized ...
... porphyrins in bulk water. D. Donner, C. Böttcher, C. Messerschmidt, U. Siggel, and J.-H. Fuhrhop - 1999. ...
The structure presents a rare example for a planar nickel(II) porphyrin, as meso-substituted nickel(II) porphyrins with either ... Senge, M.O., Davis, M, (5,15-Dianthracen-9-yl-10,20-dihexyl-porphyrinato)nickel(II): A planar nickel(II) porphyrin, Acta ... The title compound, [Ni(C60H52N4)], is an example of a meso tetrasubstituted nickel(II) porphyrin with both meso aryl and alkyl ... 5,15-Dianthracen-9-yl-10,20-dihexyl-porphyrinato)nickel(II): A planar nickel(II) porphyrin. ...
Porphyrins with carboxylic acid functional groups as active sites for linkage of the porphyrin to TiO2 and aminophenyl groups ... The desired functional porphyrin 5, 10, 15-tri-( 4-carboxyphenyl)-20-( 4- aminophenyl)porphyrin (TC3APP), which will be used as ... An unsymmetrical porphyrin, 5,10,15-tri-[4-(carbomethoxy)phenyl]-20- [(4-acetamido)phenyl]porphyrin (TCM3AAPP), with two ... Reaction conditions for synthesis of the parent porphyrin have been optimized by HPLC analysis. The desired porphyrin TC3APP ...
Title: Manipulation of the magnetic state of a porphyrin-based molecule on gold: From Kondo to quantum nanomagnet via the ... Abstract: By moving individual Fe-Porphyrin-based molecules with the tip of Scanning Tunneling Microscope in the vicinity of a ...
The best porphyrin structure Ive seen for a while is right there in Early View - Harry Anderson and cohorts in Oxford have ... used a porphyrin to template the formation of a conjugated octaporphyrin ring (thought Id mention this before carbon-based ...
Porphyrins, Blood and Urine answers are found in the Daviss Lab & Diagnostic Tests powered by Unbound Medicine. Available for ... "Porphyrins, Blood and Urine." Daviss Lab & Diagnostic Tests, 7th ed., F.A. Davis Company, 2017. Nursing Central, nursing. ... Porphyrins, Blood and Urine [Internet]. In: Daviss Lab & Diagnostic Tests. F.A. Davis Company; 2017. [cited 2023 September 23 ... Van Leeuwen, A. M., & Bladh, M. L. (2017). Porphyrins, Blood and Urine. In Daviss Lab & Diagnostic Tests (7th ed.). F.A. Davis ...
Title: Facile Supramolecular Engineering of Porphyrin cis Tautomers: The Case of β-Octabromo- meso -tetraarylporphyrins ... Facile Supramolecular Engineering of Porphyrin cis Tautomers: The Case of β-Octabromo- meso -tetraarylporphyrins. ACS Omega, 5 ... Accepted Manuscript: Facile Supramolecular Engineering of Porphyrin cis Tautomers: The Case of β-Octabromo- meso - ... "Facile Supramolecular Engineering of Porphyrin cis Tautomers: The Case of β-Octabromo- meso -tetraarylporphyrins". ACS Omega 5 ...
Weak complexes between the iron porphyrin nitrosyls and the pyridines or amines were observed. Upon reduction, the pyridine or ... Choi, In Kyu and Ryan, Michael D., "The Electrochemistry of Iron Porphyrin Nitrosyls in the Presence of Pyridines and Amines" ( ... Weak complexes between the iron porphyrin nitrosyls and the pyridines or amines were observed. Upon reduction, the pyridine or ... The Electrochemistry of Iron Porphyrin Nitrosyls in the Presence of Pyridines and Amines. ...
Alfa Chemistry can provide Porphyrin MOFs Ligands for customers. ... Porphyrin MOFs Ligands. CAS. Product Name. Inquiry. 10170-03-3 ... Tetra(3,5-dibromo-4-hydroxyphenyl)porphyrin. Inquiry. 1270214-59-9. 5,10,15,20-Tetrakis[4-(1,3,2-dioxaborinan- 2-yl)phenyl]-21H ... 5,10,15,20-Tetrakis(4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)porphyrin. Inquiry. ...
A blog post on research looking at a link between autism and porphyrins ... the porphyrins.. Ill readily admit that porphyrins are not generally part of my knows what he is talking about repertoire, a ... Dobriner K. et al. The excretion of porphyrins in congenital porphyria. Journal of Clinical Investigation. 1938; 17: 761-764.. ... Id better add porphyrins to the autism research wish list.. * Pishchany G. & Skaar EP. Taste for blood: hemoglobin as a ...
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Home / Porphyrins / Pyridylporphyrins / Metalloporphyrins, Porphyrins, Pyridylporphyrins. 228,00 €. - 480,00 €. Catalog No.: ... Porphyrins Meso-Tetraphenylporphyrin-Gd(III) acetate. 354,00 €. - 494,00 €. Select options ... Porphyrins meso-Tetraphenylporphyrin-In(III) chloride. 72,00 €. - 280,00 €. Select options ... Porphyrin Systems is a company founded 1999 as a spin-off from the University of Lübeck, Germany. ...
Porphyrins (blood). Category. Biochemistry Test background. The porphyrias are inherited or acquired disorders of certain ...

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