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- W2022061860 abstract "L'action coagulante du venin de Bothrops atrox a été analysée in vitro sur du fibrinogène purifié et sur des plasmas normaux ou déficients en différents facteurs de la coagulation sanguine. Cette étude a montré que le venin de Bothrops atrox a une action « thrombin-likedue à une ou des protéases à sérine sensibles au DFP, mais que son action coagulante est en fait principalement due à des composants insensibles au DFP, qui activent la prothrombine et le facteur X (facteur Stuart). Nous avons purifié partiellement l'activateur du facteur X insensible au DFP du venin de Bothrops atrox. Dans des conditions natives, cette fraction purifiée est constituée d'une protéine de masse moléculaire 77.000 daltons, tandis que par électrophorèse sur gel de polyacrylamide en présence de SDS elle contient principalement une chaîne polypeptidique lourde (65.000) et un doublet léger (12 – 13.000). L'activateur purifié dont l'action coagulante est insensible au DFP, catalyse in vitro, de façon calcium-dépendante, la conversion du facteur X en facteur Xa. Par ses propriétés moléculaires il ressemble plus à l'activateur du venin de la vipère de Russell qu'aux activateurs physiologiques du facteur X. The coagulating activity of Bothrops atrox venom was investigated in vitro with purified fibrinogen, with normal plasma and with plasma deficient in various factors of the coagulation cascade. This study indicated that Bothrops atrox venom possesses a thrombin-like action caused by one or several serine proteases sensitive to DFP treatment, but that its clotting action is in fact mainly due to components insensitive to DFP which activate prothrombin and factor X (Stuart factor). We partially purified the DFP insensitive activator of factor X from Bothrops atrox venom and found it to be a protein of molecular weight 77,000. Analysis of the purified fraction by electrophoresis on polyacrylamide gel in the presence of SDS showed that it is mainly composed of one heavy polypeptide chain (65,000) and one light doublet (12 – 13,000). This activator is calcium-dependent and catalyzes in vitro the conversion of purified factor X into factor Xa. By its molecular properties, it resembles the factor X activator from Vipera russellii venom rather than physiological activators." @default.
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- W2022061860 date "1983-03-01" @default.
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- W2022061860 title "Blood coagulation induced by Bothrops atrox venom : Idendification and properties of a factor X activator" @default.
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- W2022061860 doi "https://doi.org/10.1016/s0300-9084(83)80085-6" @default.
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