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Abrin and Ricin: New Anti-tumour Substances
Nature, 1970Abrin and ricin are highly toxic proteins isolated and crystallized from Abrus precatorius1 and Ricinus communis respectively2–4. The LD50s of abrin and ricin are 0.020 0.012 mg/kg body weight of mice respectively. Both have a molecular weight of 65,000, but a different chemical structure as judged by the analysis of N and C terminal amino-acid ...
Jung-Yaw Lin
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Abrin and hurin: Two new lymphocyte mitogens
Cell, 1975Two plant proteins, abrin from the seed of Abrus precatorius and hurin from the seed of Hura crepitans, are potent lymphocyte mitogens. The extent of stimulation of BALB/C AND CBA strain mouse spleens by these factors is significantly greater than that attained with PHA or PWM and requires thymus-derived lymphocytes.
Alexander McPherson
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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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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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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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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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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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Toxicon, 2017
Abrin, a type II ribosome inactivating protein from the Abrus precatorius plant, is extremely toxic. It has been shown to be 75 times more potent than its infamous sister toxin, ricin and their potential use in bio-warfare is a cause of major concern.
Tiwari, Vinita +2 more
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Abrin, a type II ribosome inactivating protein from the Abrus precatorius plant, is extremely toxic. It has been shown to be 75 times more potent than its infamous sister toxin, ricin and their potential use in bio-warfare is a cause of major concern.
Tiwari, Vinita +2 more
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Distribution of I131-labeled abrin in vivo
Toxicon, 1970Abstract Abrin, the crystalline toxic protein isolated from Abrus precatorius was greatly inactivated by iodination. Two hours after i.p. injection of I131-labeled abrin, about 12 per cent of injected protein was found in liver while much less was detected in other organs.
J Y, Lin, S T, Ju, Y S, Shaw, T C, Tung
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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%.
Jung-Yaw Lin
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