A plant genus of the family FABACEAE. Members contain ABRIN.
A toxic lectin from the seeds of jequirity, Abrus precatorius L. Very active poison. Five different proteins have so far been isolated: Abrus agglutinin, the component responsible for: hemagglutinating activity, & abrins a-d, the toxic principals each consisting of two peptide chains are held together by disulfide bonds.
Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
The encapsulated embryos of flowering plants. They are used as is or for animal feed because of the high content of concentrated nutrients like starches, proteins, and fats. Rapeseed, cottonseed, and sunflower seed are also produced for the oils (fats) they yield.

Pulchellin, a highly toxic type 2 ribosome-inactivating protein from Abrus pulchellus. Cloning heterologous expression of A-chain and structural studies. (1/13)

Pulchellin is a type 2 ribosome-inactivating protein isolated from seeds of the Abrus pulchellus tenuiflorus plant. This study aims to obtain active and homogeneous protein for structural and biological studies that will clarify the functional aspects of this toxin. The DNA fragment encoding pulchellin A-chain was cloned and inserted into pGEX-5X to express the recombinant pulchellin A-chain (rPAC) as a fusion protein in Escherichia coli. The deduced amino acid sequence analyses of the rPAC presented a high sequential identity (> 86%) with the A-chain of abrin-c. The ability of the rPAC to depurinate rRNA in yeast ribosome was also demonstrated in vitro. In order to validate the toxic activity we promoted the in vitro association of the rPAC with the recombinant pulchellin binding chain (rPBC). Both chains were incubated in the presence of a reduced/oxidized system, yielding an active heterodimer (rPAB). The rPAB showed an apparent molecular mass of approximately 60 kDa, similar to the native pulchellin. The toxic activities of the rPAB and native pulchellin were compared by intraperitoneal injection of different dilutions into mice. The rPAB was able to kill 50% of the tested mice with doses of 45 microg x kg(-1). Our results indicated that the heterodimer showed toxic activity and a conformational pattern similar to pulchellin. In addition, rPAC produced in this heterologous system might be useful for the preparation of immunoconjugates with potential as a therapeutic agent.  (+info)

Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin. (2/13)

Abrin and agglutinin-I from the seeds of Abrus precatorius are type II ribosome-inactivating proteins that inhibit protein synthesis in eukaryotic cells. The two toxins share a high degree of sequence similarity; however, agglutinin-I is weaker in its activity. We compared the kinetics of protein synthesis inhibition by abrin and agglutinin-I in two different cell lines and found that approximately 200-2000-fold higher concentration of agglutinin-I is needed for the same degree of inhibition. Like abrin, agglutinin-I also induced apoptosis in the cells by triggering the intrinsic mitochondrial pathway, although at higher concentrations as compared with abrin. The reason for the decreased toxicity of agglutinin-I became apparent on the analysis of the crystal structure of agglutinin-I obtained by us in comparison with that of the reported structure of abrin. The overall protein folding of agglutinin-I is similar to that of abrin-a with a single disulfide bond holding the toxic A subunit and the lectin-like B-subunit together, constituting a heterodimer. However, there are significant differences in the secondary structural elements, mostly in the A chain. The substitution of Asn-200 in abrin-a with Pro-199 in agglutinin-I seems to be a major cause for the decreased toxicity of agglutinin-I. This perhaps is not a consequence of any kink formation by a proline residue in the helical segment, as reported by others earlier, but due to fewer interactions that proline can possibly have with the bound substrate.  (+info)

Quantification of L-abrine in human and rat urine: a biomarker for the toxin abrin. (3/13)

Abrin is a toxic protein found in the jequirity seed. L-Abrine (N-methyl-tryptophan) is also found in the jequirity seed and can be used as a biomarker for abrin exposure. Analysis of L-abrine was added to an existing method for quantifying ricinine as a marker for ricin exposure in human urine and analytically validated. Accuracy and reproducibility were enhanced by including a newly synthesized (13)C(1)(2)H(3)-L-abrine internal standard. One-milliliter urine samples were processed using solid-phase extraction prior to a 6-min high-performance liquid chromatography separation. Protonated molecular ions were formed via electrospray ionization in a triple-quadrupole mass spectrometer and quantified via multiple reaction monitoring. Method validation included the characterization of two enriched urine pools, which were used as quality control materials. Endogenous levels of L-abrine were quantified in a reference range of 113 random urine samples at 0.72 +/- 0.51 ng/mL. Urinary concentrations of L-abrine were monitored in an intentional rat exposure study for up to 48 h. Comparing the results from the human reference range and the animal exposure study indicates that this method is suitable for quantifying L-abrine within 24 h post-exposure. Quantification of L-abrine beyond 24 h is limited by rapid excretion of the biomarker and the level of the L-abrine dose.  (+info)

A biophysical elucidation for less toxicity of agglutinin than abrin-a from the seeds of Abrus precatorius in consequence of crystal structure. (4/13)

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Attempted suicide, by mail order: Abrus precatorius. (5/13)

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A recombinant mutant abrin A chain expressed in Escherichia coli can be used as an effective vaccine candidate. (6/13)

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The role of the C-terminal region of pulchellin A-chain in the interaction with membrane model systems. (7/13)

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A new triterpenoid saponin from Abrus precatorius Linn. (8/13)

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'Abrus' is a term that refers to a genus of plants in the pea family (Fabaceae), specifically to the tropical and subtropical species of the genus *Abrus*. The most well-known species is *Abrus precatorius*, also known as Jequirity, Crab's Eye, or Rosary Pea. This plant has gained notoriety due to its seeds, which contain a potent toxin called abrin.

The abrin toxin is found in the seeds' endosperm and is extremely toxic if ingested or even handled and then accidentally introduced into the body through mucous membranes or broken skin. It functions by inhibiting protein synthesis within cells, leading to cell death and potentially severe health consequences, including organ failure and even death in extreme cases.

It's important to note that all parts of the *Abrus* plant contain toxic compounds, but the seeds are particularly dangerous due to their high concentration of abrin. The seeds are often used in jewelry or rosaries, and great care should be taken when handling them to avoid exposure to the toxin.

Abrin is a protein toxin found in the seeds of the rosary pea plant (Abrus precatorius), also known as jequirity bean. It is a highly potent toxin, similar in structure and function to ricin, which is found in castor beans. Abrin inhibits protein synthesis in cells by removing a critical adenine residue from the 28S rRNA of the 60S ribosomal subunit, thereby preventing peptide bond formation and ultimately leading to cell death.

Ingesting or inhaling abrin can cause severe illness or death in both humans and animals. Symptoms of abrin poisoning may include nausea, vomiting, diarrhea, abdominal pain, and fever, followed by respiratory distress, multi-organ failure, and potentially fatal shock. There is no antidote for abrin poisoning, and treatment is primarily supportive, focusing on managing symptoms and maintaining vital organ function.

It's important to note that abrin is classified as a potential bioterrorism agent due to its high toxicity and potential use in malicious attacks. As such, handling or coming into contact with abrin should be avoided, and any suspected exposure should be reported to medical professionals immediately.

Plant lectins are proteins or glycoproteins that are abundantly found in various plant parts such as seeds, leaves, stems, and roots. They have the ability to bind specifically to carbohydrate structures present on cell membranes, known as glycoconjugates. This binding property of lectins is reversible and non-catalytic, meaning it does not involve any enzymatic activity.

Lectins play several roles in plants, including defense against predators, pathogens, and herbivores. They can agglutinate red blood cells, stimulate the immune system, and have been implicated in various biological processes such as cell growth, differentiation, and apoptosis (programmed cell death). Some lectins also exhibit mitogenic activity, which means they can stimulate the proliferation of certain types of cells.

In the medical field, plant lectins have gained attention due to their potential therapeutic applications. For instance, some lectins have been shown to possess anti-cancer properties and are being investigated as potential cancer treatments. However, it is important to note that some lectins can be toxic or allergenic to humans and animals, so they must be used with caution.

Lectins are a type of proteins that bind specifically to carbohydrates and have been found in various plant and animal sources. They play important roles in biological recognition events, such as cell-cell adhesion, and can also be involved in the immune response. Some lectins can agglutinate certain types of cells or precipitate glycoproteins, while others may have a more direct effect on cellular processes. In some cases, lectins from plants can cause adverse effects in humans if ingested, such as digestive discomfort or allergic reactions.

In medical terms, "seeds" are often referred to as a small amount of a substance, such as a radioactive material or drug, that is inserted into a tissue or placed inside a capsule for the purpose of treating a medical condition. This can include procedures like brachytherapy, where seeds containing radioactive materials are used in the treatment of cancer to kill cancer cells and shrink tumors. Similarly, in some forms of drug delivery, seeds containing medication can be used to gradually release the drug into the body over an extended period of time.

It's important to note that "seeds" have different meanings and applications depending on the medical context. In other cases, "seeds" may simply refer to small particles or structures found in the body, such as those present in the eye's retina.

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