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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 ...
Lin, J +4 more
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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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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.
S J, Kaufman, A, McPherson
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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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Abrin and ricin — two toxic lectins
Trends in Biochemical Sciences, 1978Abrin and ricin are two peculiar proteins, each having two peptide chains with different functions. One chain, the ‘effectomer', is an enzyme capable of inactivating eucaryotic ribosomes. The other chain, the ‘huptomer', is a lectin which binds the toxin to cells and facilitates the entry of the effectomer into the cytoplasm.
Sjur Olsnes, Alexander Pihl
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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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Massive fatal overdose of abrin with progressive encephalopathy
Clinical Toxicology, 2019Introduction: The jequirity bean (Abrus precatorius) seed contains abrin, a toxalbumin, that irreversibly binds the 60-s ribosomal subunit inhibiting protein synthesis. Neurologic manifestations of ingestions are rare.Case details: We present a case of a 20-year-old man with 24 h of vomiting, diarrhea and 2 h of hematemesis and hematochezia.
B Zane, Horowitz +5 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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Abrin, Ricin, and their Associated Agglutinins
1977It has been known since ancient times that the seeds of Abrus precatorius L. (Semen Jequiriti)* and Ricinus communis L.† (castor bean) are highly toxic, and the seeds have been used in folk medicine against a wide variety of diseases and also for various non-medical purposes.
S. Olsnes, A. Pihl
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