Abrin. Medical search

A plant genus of the family FABACEAE. Members contain ABRIN.

A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally.

Ribosome inactivating proteins consisting of two polypeptide chains, the toxic A subunit and a lectin B subunit, linked by disulfide bridges. The lectin portion binds to cell surfaces and facilitates transport into the ENDOPLASMIC RETICULUM.

A plant genus of the family EUPHORBIACEAE, order Euphorbiales, subclass Rosidae. The seed of Ricinus communis L. is the CASTOR BEAN which is the source of CASTOR OIL; RICIN; and other lectins.

Specific, characterizable, poisonous chemicals, often PROTEINS, with specific biological properties, including immunogenicity, produced by microbes, higher plants (PLANTS, TOXIC), or ANIMALS.

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.

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.

Semisynthetic conjugates of various toxic molecules, including RADIOACTIVE ISOTOPES and bacterial or plant toxins, with specific immune substances such as IMMUNOGLOBULINS; MONOCLONAL ANTIBODIES; and ANTIGENS. The antitumor or antiviral immune substance carries the toxin to the tumor or infected cell where the toxin exerts its poisonous effect.

A disaccharide of GLUCOSE and GALACTOSE in human and cow milk. It is used in pharmacy for tablets, in medicine as a nutrient, and in industry.

Plant-derived ribosome-inactivating protein (RIP) purified from the Chinese medicinal herb tian-hua-fen which is obtained from the root tubers of Trichosanthes kirilowii. It has been used as an abortifacient and in the treatment of trophoblastic tumors. GLQ223 (Compound Q), a highly purified form of trichosanthin, has been proposed as antiviral treatment for AIDS.

Parasitic plants that form a bushy growth on branches of host trees which are in the order Santalales. It includes the Christmas mistletoe family (VISCACEAE), the showy mistletoe family (LORANTHACEAE) and the catkin mistletoe family (Eremolepidaceae). The composition of toxins, lectins, tyramine, phenethylamines, and other compounds may be affected by the host.

Ribosome inactivating proteins consisting of only the toxic A subunit, which is a polypeptide of around 30 kDa.

Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.

Antisera from immunized animals that is purified and used as a passive immunizing agent against specific BACTERIAL TOXINS.

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.

An ADP-ribosylating polypeptide produced by CORYNEBACTERIUM DIPHTHERIAE that causes the signs and symptoms of DIPHTHERIA. It can be broken into two unequal domains: the smaller, catalytic A domain is the lethal moiety and contains MONO(ADP-RIBOSE) TRANSFERASES which transfers ADP RIBOSE to PEPTIDE ELONGATION FACTOR 2 thereby inhibiting protein synthesis; and the larger B domain that is needed for entry into cells.

Chemicals that are used to cause the disturbance, disease, or death of humans during WARFARE.

A computer simulation technique that is used to model the interaction between two molecules. Typically the docking simulation measures the interactions of a small molecule or ligand with a part of a larger molecule such as a protein.

Constituent of the 60S subunit of eukaryotic ribosomes. 28S rRNA is involved in the initiation of polypeptide synthesis in eukaryotes.

Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.

A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.

Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.

A phenothiazine with actions similar to CHLORPROMAZINE. It is used as an antipsychotic and an antiemetic.

Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.

Glycoprotein molecules on the surface of B- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.

The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.

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.

Protein factors uniquely required during the elongation phase of protein synthesis.

An aldohexose that occurs naturally in the D-form in lactose, cerebrosides, gangliosides, and mucoproteins. Deficiency of galactosyl-1-phosphate uridyltransferase (GALACTOSE-1-PHOSPHATE URIDYL-TRANSFERASE DEFICIENCY DISEASE) causes an error in galactose metabolism called GALACTOSEMIA, resulting in elevations of galactose in the blood.

Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.

The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.

The rate dynamics in chemical or physical systems.

Antibodies produced by a single clone of cells.

Methods used for studying the interactions of antibodies with specific regions of protein antigens. Important applications of epitope mapping are found within the area of immunochemistry.

The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.

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.

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.

The measurement of infection-blocking titer of ANTISERA by testing a series of dilutions for a given virus-antiserum interaction end-point, which is generally the dilution at which tissue cultures inoculated with the serum-virus mixtures demonstrate cytopathology (CPE) or the dilution at which 50% of test animals injected with serum-virus mixtures show infectivity (ID50) or die (LD50).

The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.

Established cell cultures that have the potential to propagate indefinitely.

The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

Proteins prepared by recombinant DNA technology.

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.

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 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 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.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding. (1/73)

The effects of pH and ligand binding on the stability of abrin II, a heterodimeric ribosome-inactivating protein, and its subunits have been studied using high-sensitivity differential scanning calorimetry. At pH7.2, the calorimetric scan consists of two transitions, which correspond to the B-subunit [transition temperature (Tm) 319.2K] and the A-subunit (Tm 324.6K) of abrin II, as also confirmed by studies on the isolated A-subunit. The calorimetric enthalpy of the isolated A-subunit of abrin II is similar to that of the higher-temperature transition. However, its Tm is 2.4K lower than that of the higher-temperature peak of intact abrin II. This indicates that there is some interaction between the two subunits. Abrin II displays increased stability as the pH is decreased to 4.5. Lactose increases the Tm values as well as the enthalpies of both transitions. This effect is more pronounced at pH7.2 than at pH4.5. This suggests that ligand binding stabilizes the native conformation of abrin II. Analysis of the B-subunit transition temperature as a function of lactose concentration suggests that two lactose molecules bind to one molecule of abrin II at pH7.2. The presence of two binding sites for lactose on the abrin II molecule is also indicated by isothermal titration calorimetry. Plotting DeltaHm (the molar transition enthalpy at Tm) against Tm yielded values for DeltaCp (change in excess heat capacity) of 27+/-2 kJ.mol-1.K-1 for the B-subunit and 20+/-1 kJ.mol-1.K-1 for the A-subunit. These values have been used to calculate the thermal stability of abrin II and to surmise the mechanism of its transmembrane translocation. (+info)

Restoration of lectin activity to an inactive abrin B chain by substitution and mutation of the 2 gamma subdomain. (2/73)

Abrin is a heterodimeric plant protein that occurs in several isoforms (abrin-a, abrin-b, abrin-c and abrin-d), whose B chains are believed to either have (abrin-a and abrin-d) or lack (abrin-b and abrin-c) the ability to bind galactose. The 5' signal sequence and toxin B chain (ATB)-coding region were excised from a preproabrin cDNA [K. A. Wood, J. M. Lord, E. J. Wawrzynczak, and M. Piatak (1991) Eur. J. Biochem. 198, 723-732], tentatively identified as abrin-c, which was predicted to lack lectin activity, and fused in-frame to generate pre-ATB cDNA. Transcripts, synthesized in vitro from pre-ATB cloned into the transcription vector pSP64T, were expressed after microinjection into Xenopus oocytes. The recombinant ATB was shown, using a qualitative sugar-binding assay, to be devoid of lectin activity. Lectin activity could not be restored to this nonbinding ATB by replacing the 2 gamma subdomain with the corresponding galactose-binding 2 gamma subdomain from ricin B chain, but it was restored by replacement with the active galactose-binding 2 gamma subdomain from a different abrin isoform (abrin-a). The putative galactose-binding pocket of the nonbinding ATB 2 gamma subdomain contained a His residue at the position occupied by a residue with an aromatic side chain (Tyr or Trp) in functional 2 gamma subdomains. Mutationally converting this His to either Tyr or Trp restored lectin activity to the nonbinding ATB, emphasizing the contribution of an aromatic side chain in a functional 2 gamma subdomain galactose-binding site for members of this lectin family. (+info)

Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: structural similarity to the B-chain from plant lectin, ricin. (3/73)

CEL-III, a galactose/N-acetylgalactosamine (Gal/GalNAc) specific lectin purified from a marine invertebrate Cucumaria echinata has a strong hemolytic activity especially toward human and rabbit erythrocytes. We determined the primary structure of the CEL-III by examining the amino acid sequences of the protein and the nucleotide sequence of the cDNA. The cDNA encoding CEL-III has 1823 nucleotides and an open reading frame of 1296 nucleotides. CEL-III is composed of 432 amino acid residues with a M(r) of 47 inverted question mark omitted inverted question mark457 and has six internal tandem repeats, each with of 40-50 amino acids, comprising the N-terminal two-thirds of the molecule. Similar repeats are found in the B-chains of cytotoxic plant lectins, such as ricin and abrin, where six repetitive sequences extend throughout the molecules. A hydropathy plot predicts hydrophobic segments in the C-terminal region of CEL-III. These findings suggest that the N-terminal region of CEL-III plays an important role in binding to carbohydrate receptors on the target cell membranes, an event which triggers an intermolecular hydrophobic interaction of the C-terminal region, the result being oligomerization of CEL-III to lead to pore-formation in erythrocyte membrane. (+info)

Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity. (4/73)

Abrus agglutinin (AAG), a low-toxicity protein from the plant Abrus precatorius, is less lethal than abrina (ABRa) in mice (LD(50) = 5 mg/kg versus 20 microg/kg of body weight). Nucleotide sequence analysis of a cDNA clone encoding full-length AAG showed an open reading frame with 1641 base pairs, corresponding to a 547-amino acid residue preproprotein containing a signal peptide and a linker region (two amino acid residues) between the AAG-A and AAG-B subunits. AAG had high homology to ABRa (77.8%). The 13 amino acid residues involved in catalytic function, which are highly conserved among abrins and ricins, were also conserved within AAG-A. The protein synthesis inhibitory activity of AAG-A (IC(50) = 3.5 nM) was weaker than that of ABRa-A (0.05 nM). Molecular modeling followed by site-directed mutagenesis showed that Pro(199) of AAG-A, located in amphiphilic helix H and corresponding to Asn(200) of ABRa-A, can induce bending of helix H. This bending would presumably affect the binding of AAG-A to its target sequence, GpApGpAp, in the tetraloop structure of the 28 S rRNA subunit and could be one of the major factors contributing to the relatively weak protein synthesis inhibitory activity and toxicity of AAG. (+info)

Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. (5/73)

Abrin A-chain (ABRA) inhibits protein synthesis by its N-glycosidase activity as well as induces apoptosis, but the molecular mechanism of ABRA-induced cell death has been obscure. Using an ABRA mutant that lacks N-glycosidase activity as bait in a yeast two-hybrid system, a 30-kDa antioxidant protein-1 (AOP-1) was found to be an ABRA(E164Q)-interacting protein. The interaction was further confirmed in vitro by a glutathione S-transferase pull-down assay. The colocalization of endogenous AOP-1 and exogenous ABR proteins in the cell was demonstrated by confocal immunofluorescence. We also demonstrated that ABRA attenuates AOP-1 antioxidant activity in a dose-dependent manner and the intracellular level of reactive oxygen species (ROS) increases in ABR-treated cells. Moreover, ROS scavengers N-acetylcysteine and 4-hydroxy-2,2,6,6-tetramethylpiperidine-1-oxyl delayed programmed cell death. This indicates that ROS are important mediators of ABR-induced apoptosis. When ectopically expressed, AOP-1 blocked the release of cytochrome c and prevented apoptosis in ABR-treated cells. These findings suggest that the binding of ABRA to AOP-1 promotes apoptosis by inhibiting the mitochondrial antioxidant protein AOP-1, resulting in the increase of intracellular ROS and the release of cytochrome c from the mitochondria to the cytosol, which activates caspase-9 and caspase-3. (+info)

Ribosome inactivation by the toxic lectins abrin and ricin. Kinetics of the enzymic activity of the toxin A-chains. (6/73)

A sensitive test system for toxin-treated ribosomes was worked out by treating rabbit reticulocyte ribosomes with abrin A-chain, ricin A-chain or ricinus agglutinin A-chain, adding neutralizing amounts of specific antitoxins and testing for polyphenylalanine-synthesizing activity in a system where the concentration of elongation factors and ribosomes were varied. The strongest inhibition was obtained in the presence of low concentrations of elongation factor (EF-2). The activity of the ribosomes decreased with time of incubation with the toxin A-chains. Addition of anti-toxins stopped further inactivation. In systems containing untreated and toxin-treated ribosomes the ability to polymerize phenylalanine was proportional to the concentration of untreated ribosomes. There was a linear relationship between toxin A-chain concentration and the number of ribosomes inactivated per minute. The inactivation rate increased with temperature, and the estimated activation energy was 10.6 kcal (44.3 kJ). Linewaver-Burk plots of the data obtained by incubating various ribosome concentrations with toxins indicated a molecular activity of about 1500 ribosomes/minute for abrin and ricin A-chains and 100 ribosomes/minute for ricinus agglutinin A-chain. The apparent Michaelis constant was 0.1-0.2 muM for all three A-chains. The activity of the A-chains in the intact cell is discussed. (+info)

Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro. (7/73)

The eye lens small heat shock proteins (sHSP), alphaA- and alphaB-crystallins, have been shown to function like molecular chaperones, both in vitro and in vivo. It is essential to assess the protective effect of alphaA- and alphaB-crystallins under native conditions to extrapolate the results to in vivo conditions. Insulin and alpha-lactalbumin have widely been used to investigate the chaperone mechanism of alpha-crystallin under native conditions. Due to its smaller size, insulin B-chain may not represent the binding of putative physiological substrate proteins. As it stands, the aggregation of alpha-lactalbumin and binding of alpha-crystallin to it varies under different experimental conditions. Abrin, a ribosome inactivating protein isolated from the seeds of Abrus precatorius, consists of a 30 kDa A-chain and a lectin-like B-chain of 33 kDa joined by a single disulfide bond. Reduction of the disulfide link between the two chains of abrin leads to the aggregation of the B-chain. In this study, we demonstrate that dithiothreitol (DTT)-induced aggregation of abrin B-chain could be monitored by light scattering similar to that of insulin. Moreso, this process could be suppressed by recombinant human alphaA- and alphaB-crystallins in a concentration dependent manner, notably by binding to aggregation prone abrin B-chain. SDS-PAGE and HPLC gel filtration analysis indicate that there is a soluble complex formation between alpha-crystallin and abrin B-chain. Interestingly, in contrast to insulin, there is no significant difference between alphaA- and alphaB-crystallin in suppressing the aggregation of abrin B-chain at two different temperatures (25 and 37 degrees C). HSP26, an another small heat shock/alpha-crystallin family protein, was also able to prevent the DTT-induced aggregation of abrin. These results suggest that due to relatively larger size of its B-chain (33 kDa), compared to insulin B-chain (about 3 kDa), abrin may serve as a better model substrate for in vitro chaperone studies of alpha-crystallin and as well as other sHSP. (+info)

Cloning, expression of the abrin-a A-chain in Escherichia coli and measurement of the biological activities in vitro. (8/73)

The coding sequence of abrin-a A-chain (ABRaA) gene was obtained by RT-PCR and cloned into the expression vector pET28b. The mature ABRaA has been highly expressed in the cytoplasm of Escherichia coli by 1 mmol/L IPTG induction, and the yield of the soluble recombinant protein was 4 mg/L of induced culture. The recombinant ABRaA was purified to be homogeneity. The biological activities of expressed ABRaA were demonstrated in vitro. It strongly inhibited the protein biosynthesis of rabbit reticulocyte lysates, with an IC(50) of 0.08 nmol/L. It also depurinated 28 S rRNA through cleaving at the A4324 site in rat liver ribosomes by its N-glycosidase activity. These data suggested that the recombinant ABRaA could be used for the preparation of immunotoxins as a potential cancer chemotherapeutic agent. (+info)

... but abrin's effect is more potent than ricin's. The toxic effect of abrin is due to an intracellular, multi-step process. Abrin ... A molecule of abrin-a has a total of 528 amino acids and is about 65 kDa in mass. Abrin-a is formed after the cleavage of a ... Abrin is classed as a "select agent" under U.S. law. Abrin is only formed in nature by the rosary pea. The brightly coloured ... Abrin is a water-soluble lectin. Abrin in powdered form is yellowish-white. It is a stable substance and can withstand extreme ...

https://en.wikipedia.org/wiki/Abrin

Abrin , Abtar , Abzan , Achkidar , Achu Bazar , Adamabad-e Baluchi Now , Adelabad , Adernag , Adimi , Adireh , Afghan , ...

https://en.wikipedia.org/wiki/List_of_cities,_towns_and_villages_in_Sistan_and_Baluchestan_Province

ISBN 978-0-8247-8374-7. Lin JY, Chen CC, Lin LT, Tung TC (June 1969). "Studies on the toxic action of abrin". Taiwan Yi Xue Hui ... Fodstad O, Johannessen JV, Schjerven L, Pihl A (November 1979). "Toxicity of abrin and ricin in mice and dogs". Journal of ... Wiley RG, Stirpe F (January 1988). "Modeccin and volkensin but not abrin are effective suicide transport agents in rat CNS". ... Olsnes S, Pihl A (May 1973). "Isolation and properties of abrin: a toxic protein inhibiting protein synthesis. Evidence for ...

https://en.wikipedia.org/wiki/Modeccin

Typical toxalbumins are abrin and ricin.[self-published source?] Ingestion of seed containing toxalbumins is not necessarily ...

https://en.wikipedia.org/wiki/Toxalbumin

Fūrin Kazan (風林火山) is the 46th NHK Taiga drama television series that began on January 7, 2007. It was aired throughout 2007, with the last episode aired December 16, 2007. Its official English title is The Trusted Confidant. The story, to a large extent, was an adaptation of Yasushi Inoue's 1959 historical novel of the same title (published in English under the title The Samurai Banner of Furin Kazan). The four characters of the title, from left to right are wind, woods, fire, and mountain. The title is a reference to the war banner used by Takeda Shingen, which in turn was taken from Sun Tzu's The Art of War. It means "Swift as the Wind, Silent as a Forest, Fierce as Fire and Immovable as a Mountain." Set in the Sengoku period, it depicts the life of Yamamoto Kansuke who is known as one of Takeda Shingen's renowned strategists. Production Credits Director - Kazuhiko Shimizu Screenwriter - Sumio Ōmori Based on the novel by - Yasushi Inoue Narrator - Sachiko Kagami Music - Akira Senju ...

https://en.wikipedia.org/wiki/Fūrin_Kazan_(TV_series)

... abrin. The seeds have been used in India to kill cattle and in homicides. Captain F. C. Briggs, adjutant to General Reginald ...

https://en.wikipedia.org/wiki/Ground_glass

He accustomed mice to the poisons ricin and abrin. After feeding them with small but increasing dosages of ricin he ascertained ... Ehrlich rejected inheritance in the genetic sense because the offspring of a male mouse immunized against abrin and an ... but mice immunized against ricin were just as sensitive to abrin as untreated animals. This was followed by investigations on ... untreated female mouse were not immune to abrin. He concluded that the fetus was supplied with antibodies via the pulmonary ...

https://en.wikipedia.org/wiki/Paul_Ehrlich

SFIDA! për Shqipërinë (CHALLENGE! for Albania or simply SFIDA!) is an Albanian political party, founded in 2016. SFIDA is an anti-establishment party that promotes direct democracy, mandate limitation and vetting for politicians. SFIDA is a follow-up of the movement "Ne, Tirana" which supported Gjergj Bojaxhi during local elections in 2015 where he ran as an independent candidate for Tirana's city hall. The party does not have a traditional leader. Instead this role is split between an administrative chairman (held by Hektor Ruci) and a political representative, Gjergj Bojaxhi. In June 2015, Bojaxhi ran as an independent candidate in the local elections for the city hall of Tirana. This candidacy was supported by an organized civil movement called "Ne, Tirana". The elections were won by Erion Veliaj, however Bojaxhi won over 16,000 votes. Based on this significant public support, in 2016 Bojaxhi and several other founders created "SFIDA! për Shqipërinë" in order to extend "Ne, Tirana" to a ...

https://en.wikipedia.org/wiki/Sfida_për_Shqipërinë

"On the mechanism of protein-synthesis inhibition by abrin and ricin. Inhibition of the GTP-hydrolysis site on the 60-S ...

https://en.wikipedia.org/wiki/List_of_poisonous_plants

Shih SF, Wu YH, Hung CH, Yang HY, Lin JY (2001). "Abrin triggers cell death by inactivating a thiol-specific antioxidant ...

https://en.wikipedia.org/wiki/PRDX3

The Latin botanical Abrus is the parent of the chemical name Abrin; see abrine @ CNRTL.fr. The Arabic لبلاب lablāb means any ...

https://en.wikipedia.org/wiki/List_of_English_words_of_Arabic_origin

The toxin abrin is a dimer consisting of two protein subunits, termed A and B. The B chain facilitates abrin's entry into a ... One molecule of abrin will inactivate up to 1,500 ribosomes per second. Symptoms are identical to those of ricin, except abrin ... Abrin has an LD50 of only 0.56 μg/kg in mice, and Kingsbury lists a toxic dose in humans at 0.00015% body weight, or ... though the abrin in ingested seeds may be absorbed much more slowly than the ricin in Ricinus communis even if the seeds are ...

https://en.wikipedia.org/wiki/Abrus_precatorius

In terms of structure, ricin closely resembles abrin-a, an isotoxin of abrin. The quaternary structure of ricin is a globular, ... Kuntal Patel from London attempted to poison her mother with abrin after the latter interfered with her marriage plans. Daniel ...

https://en.wikipedia.org/wiki/Ricin

The "biological agents" were a small non-lethal amount of abrin and sodium cyanide. Per Chamberlain, he had purchased the abrin ...

https://en.wikipedia.org/wiki/Ryan_Chamberlain

Among the RIPs are some of the most toxic molecules known, including ricin and abrin. These toxins contain a second protein ...

https://en.wikipedia.org/wiki/Saporin

The structure of this protein is very similar to other RIPs, showing the most resemblance to ricin and abrin. Some birds have ...

https://en.wikipedia.org/wiki/Viscum_album

In 1897, Paul Ehrlich showed that antibodies form against the plant toxins ricin and abrin, and proposed that these antibodies ...

https://en.wikipedia.org/wiki/Humoral_immunity

Abrin from the jequirity pea is similar: One domain is a lectin that binds cell surface galactosyl residues and enables the ...

https://en.wikipedia.org/wiki/Lectin

Examples include: Abrin Beetin Ricin Saporin Shiga toxin A Spiroplasma toxin Trichosanthin Viscumin (European mistletoe) ... and abrin) ribosome inactivating proteins (RIPs). All these toxins are structurally related. RIPs have been of considerable ...

https://en.wikipedia.org/wiki/Ribosome-inactivating_protein

Abrin Botulinum neurotoxins* Clostridium perfringens epsilon toxin Conotoxins Ricin Saxitoxin Staphylococcal enterotoxins ...

https://en.wikipedia.org/wiki/Select_agent

During the Brazilian toyfare ABRIN in 2009, they presented the first product of this partnership,a 1/6th scale sculpture of the ...

https://en.wikipedia.org/wiki/Iron_Studios

Mephenytoin 1-Methyltryptophan Abrin abrine N methyl tryptophan , alkaloid in Abrus Normelatonin Phenylpiracetam Primidone ...

https://en.wikipedia.org/wiki/C12H14N2O2

No data available that match "abrin"

Abrin, like the similar plant toxin ricin, causes toxicity by inhibiting the formation (synthesis) of proteins in the cells of the exposed individual. (cdc.gov)
Abrin (and ricin) may cause severe allergic reactions. (cdc.gov)
Abrin is similar to ricin, a toxin that also is found in the seeds of a plant (the castor bean plant). (cdc.gov)
Ricin, crotin and abrin are phytotoxins. (pediatriconcall.com)
es bilden sich Antikörper gegen die Pflanzengifte Ricin, Abrin. (gesundohnepillen.de)
Similar to ricin, the rosary pea contains abrin, one of the deadliest toxins on the planet. (thealternativedaily.com)

Exposure to even a small amount of abrin may be fatal. (cdc.gov)
Someone who swallows a significant amount of abrin would develop vomiting and diarrhea that may become bloody. (cdc.gov)

Powdered abrin is yellowish-white in color. (cdc.gov)

Abrin is an extremely toxic plant protein derived from the seeds of the plant Abrus precatorius . (cdc.gov)
Abrus precatorius is a poisonous plant which contains one of the most lethal toxins, Abrin, a toxalbumin that inhibits protein synthesis causing cell death. (arubatoday.com)
Abrin is a potent toxin obtained from the seeds of Abrus precatorius. (iisc.ac.in)

Abrin can also be transmitted through the skin via small pellets or projectiles designed to carry toxin. (cdc.gov)

You could swallow (ingest) abrin if it is in food or water. (cdc.gov)
While these beans do contain a poison, it is extremely unlikely that an individual would chew through the hard shell of the seed and ingest the Abrin. (arubatoday.com)

Abrin is a natural poison that is found in the seeds of a plant called the rosary pea or jequirity pea. (cdc.gov)
The rosary pea, which is the source of abrin, is common to many tropical areas throughout the world and is sometimes used as an herbal remedy. (cdc.gov)
The seeds of the rosary pea have been used to make beaded jewelry, which can lead to abrin poisoning if the seeds are swallowed. (cdc.gov)
It would take a deliberate act to obtain abrin from rosary pea seeds and use it to poison people. (cdc.gov)

Abrin poisoning is not contagious. (cdc.gov)
Effects of abrin poisoning depend on whether abrin was breathed in, swallowed, or injected. (cdc.gov)
The major signs and symptoms of abrin poisoning depend on how someone was exposed (route of exposure) how much they were exposed to (dose). (cdc.gov)
Initial signs and symptoms of abrin poisoning by breathing in or swallowing are likely to occur within 8 hours of exposure. (cdc.gov)
Death from abrin poisoning could take place within 36 to 72 hours of exposure, depending on the route of exposure (inhalation, ingestion, or injection) and the dose received. (cdc.gov)
In the hospital, abrin poisoning is treated by giving victims supportive medical care to minimize the effects of the poisoning. (cdc.gov)

IMSEAR at SEARO: Cerebral Venous Thrombosis Due to Abrin Toxicity: A Case Report. (who.int)
Rajalakshmi K V, Shivkumar G, Karthikeyan S, Punitha V, Sangeetha K. Cerebral Venous Thrombosis Due to Abrin Toxicity: A Case Report. (who.int)

Abrin Ellis Futch, Jr, 72, passed awayMonday, October 10, 2022 at his residence under the care of GHC Hospice and surrounded by his family. (brannenkennedy.com)

The toxic component is the protein abrin that causes widespread endothelial damage. (who.int)

Within a few hours of breathing in significant amounts of abrin, the likely signs and symptoms would be difficulty breathing (respiratory distress), fever, cough, nausea, and tightness in the chest. (cdc.gov)
Showing these signs and symptoms does not necessarily mean that a person has been exposed to abrin. (cdc.gov)

Abrin can be made in the form of a powder, a mist, or a pellet, or it can be dissolved in water. (cdc.gov)
You could breathe in (inhale) abrin if it is in the form of a mist or a powder. (cdc.gov)
Skin and eye exposure: Abrin in the powder or mist form can cause redness and pain of the skin and the eyes. (cdc.gov)

Abrin is a stable substance, meaning that it can last for a long time in the environment despite extreme conditions such as very hot or very cold temperatures. (cdc.gov)

Accidental exposure to abrin is not likely. (cdc.gov)
Because no antidote exists for abrin, the most important factor is avoiding abrin exposure in the first place. (cdc.gov)
If exposure cannot be avoided, the most important factor is getting the abrin off or out of the body as quickly as possible. (cdc.gov)

Abrin ?????????? ?????? ????? ???? Heavy Speed Metal. (1bb.ru)

Water: Abrin can be used to contaminate water. (cdc.gov)
Care could include helping victims breathe, giving them intravenous fluids (fluids given through a needle inserted into a vein), giving them medications to treat conditions such as seizure and low blood pressure, administering activated charcoal (if the abrin was very recently swallowed), or washing out their eyes with water if their eyes are irritated. (cdc.gov)

Agricultural: If abrin is released into the air as fine particles (aerosol), it has the potential to contaminate agricultural products. (cdc.gov)
Abrin is used in medical research because of its potential as a treatment to kill cancer cells. (cdc.gov)
Abrin has some potential medical uses, such as in treatment to kill cancer cells. (cdc.gov)

Abrin can be absorbed into the body through ingestion, inhalation, or eye contact. (cdc.gov)
Pellets of abrin, or abrin dissolved in a liquid, could be injected into a person's body. (cdc.gov)

Abrin can be absorbed through abraded skin or through wounds, but probably not through intact skin, unless it is carried in a solvent that enhances absorption. (cdc.gov)
You could be exposed if you touch surfaces on which abrin particles or droplets have landed, or if particles or droplets of abrin land on your skin or in your eyes. (cdc.gov)

Development of PCR-Based Method for Rapid Detection of Abrin Gene', Journal of Applied Biotechnology Reports , 3(3), pp. 473-476. (biotechrep.ir)

It would take a deliberate act to obtain abrin from rosary pea seeds and use it to poison people. (cdc.gov)

Abrin, known as a ribosome inactivating protein (RIP), is a high cytotoxic plant protein. (biotechrep.ir)

Abrin 2020 reabastece o mercado nacional com grandes lançamentos! (epgrupo.com.br)

The entire A. precatorius plant contains a protein (also known as a toxalbumin) called abrin, which is considered highly toxic to humans. (webpoisoncontrol.org)

Because no antidote exists for abrin, the most important factor is avoiding abrin exposure in the first place. (cdc.gov)
There is no antidote for abrin poisoning and hospitalization is often needed to manage the symptoms. (webpoisoncontrol.org)

A Florida teen, 19-year-old Jesse William Korff, was arrested for allegedly selling one of the world's most deadly poisons, abrin, to undercover federal agents. (naturespoisons.com)

Abrin is a natural poison that is found in the seeds of a plant called the rosary pea or jequirity pea. (cdc.gov)
The seeds of the rosary pea have been used to make beaded jewelry, which can lead to abrin poisoning if the seeds are swallowed. (cdc.gov)
The plant is best known for its seeds, which are used as beads and in percussion instruments, and which are toxic due to the presence of abrin. (herbalistics.com.au)

However, abrin is considered more potent. (nih.gov)

Abrin causes illness by getting inside the cells of a person's body and preventing the cells from making the proteins they need. (cdc.gov)

Abrin can be absorbed into the body through ingestion, inhalation, or eye contact. (cdc.gov)

Inside the husk is a fatal poison called abrin. (kew.org)

Abrin is used in medical research because of its potential as a treatment to kill cancer cells. (cdc.gov)
Abrin has some potential medical uses, such as in treatment to kill cancer cells. (cdc.gov)

We used a new rapid molecular method for the detection of the abrin gene by PCR. (biotechrep.ir)

Showing these signs and symptoms does not necessarily mean that a person has been exposed to abrin. (cdc.gov)

You could swallow (ingest) abrin if it is in food or water. (cdc.gov)

9. Antitumour effect of abrin on transplanted tumours in mice. (nih.gov)

The rosary pea, which is the source of abrin, is common to many tropical areas throughout the world and is sometimes used as an herbal remedy. (cdc.gov)

Alhamdani M, Brown B, Narula P. Abrin poisoning in an 18-month-old child. (webpoisoncontrol.org)
After getting fatally poisoned by Abrin, a seven-year-old child was saved by the doctors of a private hospital in Delhi. (aninews.in)

Within a few hours of breathing in significant amounts of abrin, the likely signs and symptoms would be difficulty breathing (respiratory distress), fever, cough, nausea, and tightness in the chest. (cdc.gov)

Anatomy5

Organisms5

Diseases1

Chemicals and Drugs23

Analytical, Diagnostic and Therapeutic Techniques and Equipment4

Phenomena and Processes11

Technology, Industry, Agriculture2

Information Science4

Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding. (1/73)

Restoration of lectin activity to an inactive abrin B chain by substitution and mutation of the 2 gamma subdomain. (2/73)

Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: structural similarity to the B-chain from plant lectin, ricin. (3/73)

Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity. (4/73)

Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. (5/73)

Ribosome inactivation by the toxic lectins abrin and ricin. Kinetics of the enzymic activity of the toxin A-chains. (6/73)

Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro. (7/73)

Cloning, expression of the abrin-a A-chain in Escherichia coli and measurement of the biological activities in vitro. (8/73)

No data available that match "abrin"

Abrus

Ricin

Ribosome Inactivating Proteins, Type 2

Ricinus

Toxins, Biological

Plant Lectins

Abrin

Immunotoxins

Lactose

Trichosanthin

Mistletoe

Ribosome Inactivating Proteins, Type 1

Plant Proteins

Antitoxins

Carcinoma, Krebs 2

Lectins

Diphtheria Toxin

Chemical Warfare Agents

Molecular Docking Simulation

RNA, Ribosomal, 28S

Reticulocytes

Peptide Chain Elongation, Translational

Protein Synthesis Inhibitors

Trifluoperazine

Ribosomes

Receptors, Mitogen

Protein Biosynthesis

Seeds

Peptide Elongation Factors

Galactose

Disulfides

Biological Transport

Kinetics

Antibodies, Monoclonal

Epitope Mapping

Rabbits

Molecular Sequence Data

Amino Acid Sequence

Neutralization Tests

Cell Survival

Cell Line

HeLa Cells

Binding Sites

Models, Molecular

Recombinant Proteins

Protein Binding

Protein Conformation

Oxidation-Reduction

Escherichia coli

Base Sequence

Calorimetric studies on the stability of the ribosome-inactivating protein abrin II: effects of pH and ligand binding. (1/73)

Restoration of lectin activity to an inactive abrin B chain by substitution and mutation of the 2 gamma subdomain. (2/73)

Primary structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata and its cDNA: structural similarity to the B-chain from plant lectin, ricin. (3/73)

Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) Of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity. (4/73)

Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. (5/73)

Ribosome inactivation by the toxic lectins abrin and ricin. Kinetics of the enzymic activity of the toxin A-chains. (6/73)

Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro. (7/73)

Cloning, expression of the abrin-a A-chain in Escherichia coli and measurement of the biological activities in vitro. (8/73)

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