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• W2015778836 abstract "Human prothrombin is a single chain glycoprotein. Upon activation by factor Xa prothrombin is converted into active α-thrombin in the presence of factor Va, phospholipid and Ca++. The Echis carinatus snake venom predominantly generates meizothrombin from prothrombin, which under physiological conditions is further cleaved into α-thrombin and prothrombin fragment F1 + 2 [ 1 Morita T Iwanaga S The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venom and characterization of the new intermediates. J Biochem. 1976; 79: 1089-1108 Crossref PubMed Scopus (112) Google Scholar , 2 Morita AT, Iwanaga S. Prothrombin activator from Echis carinatus venom. Methods Enzymol 1981;80:303-11. Google Scholar ]. The physiological activation via the factor Xa/Va prothrombinase results first in formation of prethrombin 2 and fragment F1 + 2, and secondly in activation of prethrombin 2 to thrombin (Fig. 1). Thrombin plays a central role in blood coagulation including bioregulatory mechanisms like conversion of fibrinogen to fibrin, activation of platelets and blood coagulation proteins. Thrombin is irreversibly inhibited by the heparin catalyzed complex formation with the serine protease inhibitor antithrombin III." @default.
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• W2015778836 date "1997-11-01" @default.
• W2015778836 modified "2023-09-27" @default.
• W2015778836 title "Prothrombin Marburg—A Dysfunctional Coagulation Protein" @default.
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• W2015778836 doi "https://doi.org/10.1016/s0049-3848(97)00259-4" @default.
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