Results 151 to 160 of about 2,553 (186)
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Toxicological Reviews, 2003
Abrin is a toxic protein obtained from the seeds of Abrus precatorius (jequirity bean), which is similar in structure and properties to ricin. Abrin is highly toxic, with an estimated human fatal dose of 0.1-1 microgram/kg, and has caused death after accidental and intentional poisoning.
Kirsten J, Dickers +4 more
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Abrin is a toxic protein obtained from the seeds of Abrus precatorius (jequirity bean), which is similar in structure and properties to ricin. Abrin is highly toxic, with an estimated human fatal dose of 0.1-1 microgram/kg, and has caused death after accidental and intentional poisoning.
Kirsten J, Dickers +4 more
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ISOLATION OF ANTITUMOR PROTEINS ABRIN‐A AND ABRIN‐B FROM ABRUS PRECATORIUS*
International Journal of Peptide and Protein Research, 1978Two toxic proteins were purified from the seeds of Abrus precatorius by DEAE‐A 50 and Sepharose 4B chromatography. One of them does not bind on the Sepharose 4B column (Abrin‐b) and the other (Abrin‐a) is eluted with 0.2 M galactose. The amino acid compositions and tryptic maps of these two proteins were similar, but not identical.
J Y, Lin, T C, Lee, T C, Tung
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Fatal abrin poisoning by injection
Clinical Toxicology, 2020Abrin is a toxin of public health concern due to its lethality, lack of antidote, and potential for use as a bioterrorism agent. Possible routes of exposure include ingestion, inhalation, and injection. Onset of symptoms is often delayed, even in severe cases. In fatal cases, death occurs from multi-organ failure.
Ginger R, Rinner +12 more
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Radioimmunoassays of abrin and ricin in blood
Journal of Toxicology and Environmental Health, 1981Radioimmunoassays for abrin and ricin are described. There is little cross-reactivity between the two toxins. The procedures described are capable of determining blood concentrations down to 50-100 pg/ml, permitting identification of abrin and ricin poisoning and monitoring of the blood concentrations in cancer patients treated with these agents.
A, Godal, S, Olsnes, A, Pihl
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Medicine, 2007
Ricin is a type 2 ribosome-inactivating protein derived from the beans of the castor oil plant, Ricinus communis. It exerts toxicity by inhibiting protein synthesis. Many of the features seen in poisoning can be explained by ricin-induced endothelial cell damage, which leads to fluid and protein leakage and tissue oedema, causing so-called ‘vascular ...
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Ricin is a type 2 ribosome-inactivating protein derived from the beans of the castor oil plant, Ricinus communis. It exerts toxicity by inhibiting protein synthesis. Many of the features seen in poisoning can be explained by ricin-induced endothelial cell damage, which leads to fluid and protein leakage and tissue oedema, causing so-called ‘vascular ...
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Journal of Crystallographic and Spectroscopic Research, 1993
The crystal structure of abrine (N-methyl L-tryptophan, (C12H14N2O2) was determined by X-ray diffraction. Space groupP212121,a=5.372(1),b=8.595(1) andc=24.082(2)A,Z=4,D m=1.30(4) gcm−3,D x=1.304 gcm−3,R=0.039 andwR=0.042. The conformational parameters for this structure following the IUPAC nomenclature areφ=67.7(5)°, ϰ1=−175(4)°, K21=105.2(7)° and χ22=−
J. Seetharaman +2 more
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The crystal structure of abrine (N-methyl L-tryptophan, (C12H14N2O2) was determined by X-ray diffraction. Space groupP212121,a=5.372(1),b=8.595(1) andc=24.082(2)A,Z=4,D m=1.30(4) gcm−3,D x=1.304 gcm−3,R=0.039 andwR=0.042. The conformational parameters for this structure following the IUPAC nomenclature areφ=67.7(5)°, ϰ1=−175(4)°, K21=105.2(7)° and χ22=−
J. Seetharaman +2 more
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Crystal Structure of Abrin-a at 2.14 Å
Journal of Molecular Biology, 1995The crystal structure of abrin-a, a type II ribosome-inactivating protein from the seeds of Abrus precatorius, has been determined from a novel crystalline form by the molecular replacement method using the coordinates of ricin. The structure has been refined at 2.14 A to a R-factor of 18.9%.
T H, Tahirov +4 more
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Toxicity of abrin and ricin in mice and dogs
Journal of Toxicology and Environmental Health, 1979Mice and dogs, were treated iv with the cytostatic proteins abrin and ricin and observed for clinical, biochemical, and morphological aberrations. In both mice and dogs death occurred within a narrow dose range. Dogs given toxic doses of ricin and abrin showed weakness, anorexia, apathy, and moderate fever.
O, Fodstad +3 more
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Journal of Toxicology: Toxin Reviews, 1994
AbstractA family of toxic proteins, the isoabrins, which possess N-glycosylase activity toward eukaryotic 28S rRNA, may have potential use in cancer chemotherapy. By polymerase chain reaction techniques, cDNA clones of three isoabrins, carrying A and B-chain sequences, were isolated and their nucleotide sequences were determined.
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AbstractA family of toxic proteins, the isoabrins, which possess N-glycosylase activity toward eukaryotic 28S rRNA, may have potential use in cancer chemotherapy. By polymerase chain reaction techniques, cDNA clones of three isoabrins, carrying A and B-chain sequences, were isolated and their nucleotide sequences were determined.
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Sensitivity of Preimplantation Mouse Embryos to Abrin
Acta Pharmacologica et Toxicologica, 1985Abstract: The effect of the plant toxin abrin on preimplantation mouse embryos in vitro was studied. Two–cell embryos from C57BL/6J or B6CBA/Fl/Bom ♀ × B6CBA/Fl/Bom ♂ mice were exposed to abrin for 72 hrs in vitro, in medium containing abrin in concentrations ranging from 0.1 to 10,000 pg/ml.
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