Results 161 to 170 of about 3,204 (212)

Ultrafast protein digestion using an immobilized enzyme reactor following high-resolution mass spectrometry analysis for rapid identification of abrin toxin.

In Analysis
Abrin toxin, highly dangerous with an estimated human lethal dose of 0.1-1 μg per kg body weight, has attracted much attention regarding criminal and terroristic misuse over the past decade.
Meng Chen, Baoqiang Li, Wenlu Wei, Zhongyao Zhang, Lin Zhang, Cuiping Li, Qibin Huang   +6 more
semanticscholar   +1 more source

Toxicity of abrin and ricin in mice and dogs

Journal of Toxicology and Environmental Health, 1979
Mice 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, J V, Johannessen, L, Schjerven, A, Pihl   +3 more
openaire   +2 more sources

From folk remedy to toxic emergency: a case of acute abrin toxicity

Drug and chemical toxicology (New York, N.Y. 1978)
Introduction Abrus precatorius (rosary pea) contains abrin, a highly potent ribosome-inhibiting toxin. Its seeds are well-known to be toxic when chewed or crushed, while boiled seed decoctions are occasionally used in traditional medicine. Case report We
Ahmed Maher Ali, N. Zawilla, A. M. Samir, M. M. Fouad, Ahmed Negm   +4 more
semanticscholar   +1 more source

Design and evaluation of DNA aptamers with "stem-loop-chain" structures for spectrum neutralization of ricin and abrin.

Bioorganic chemistry (Print)
Ricin and abrin are classified as Type II ribosome-inactivating proteins (RIPs) toxins, posing significant potential threats to public safety and in bioterrorism incidents.
Zhenfang Xu, Jiawei Zhang, Shuangshuang Liu, Xiwei Wang, Yunhui Chen, Feiyan Wang, Xueling Ma, Weiguo Shi, Aiping Zheng, Jianchun Li, Liang Xu   +10 more
semanticscholar   +1 more source

Massive fatal overdose of abrin with progressive encephalopathy*

Clinical toxicology, 2020
Introduction: 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.
B. Horowitz, R. Castelli, Adrienne R. Hughes, R. Hendrickson, Rudolph C. Johnson, Jerry D. Thomas   +5 more
semanticscholar   +1 more source

Antitumor Protein: Abrin

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.
openaire   +1 more source

Distribution of I131-labeled abrin in vivo

Toxicon, 1970
Abstract 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
openaire   +2 more sources

Real-time and in-situ monitoring of Abrin induced cell apoptosis by using SERS spectroscopy.

Talanta: The International Journal of Pure and Applied Analytical Chemistry, 2019
Abrin is a cytotoxic protein isolated from seeds of leguminous plants and has become a potential bioterrorism weapon for its high toxity and difficult detection. In the early stage of poisoning, Arbin can damage cells and induce apoptosis.
Jingna Zhang, Xiaoyuan Ma, Zhouping Wang
semanticscholar   +1 more source

Sensitivity of Preimplantation Mouse Embryos to Abrin

Acta Pharmacologica et Toxicologica, 1985
Abstract: 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.
openaire   +2 more sources

Probing the Domain Structure of Abrin‐a by Tryptic Digestion

European Journal of Biochemistry, 1996
Abrin‐a is a potent plant toxin that consists of A and B chains linked by a disulfide bond. The abrin‐a A chain (AaTA) has N‐glycosidase activity while the abrin‐a B chain (AaTB) has galactose‐binding activity. By partial tryptic digestion, the domain structure of abrin‐a was investigated. Seven tryptic fragments with molecular masses greater than 3500
S H, Lin, L P, Chow, Y L, Chen, Y C, Liaw, J K, Chen, J Y, Lin   +5 more
openaire   +2 more sources