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Authors = Rodney M. Camire

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Open AccessReview Procoagulant Adaptation of a Blood Coagulation Prothrombinase-like Enzyme Complex in Australian Elapid Venom
Toxins 2010, 2(6), 1554-1567; doi:10.3390/toxins2061554
Received: 30 March 2010 / Revised: 4 June 2010 / Accepted: 17 June 2010 / Published: 18 June 2010
Cited by 5 | Viewed by 4426 | PDF Full-text (756 KB) | HTML Full-text | XML Full-text
Abstract
The macromolecular enzyme complex prothrombinase serves an indispensable role in blood coagulation as it catalyzes the conversion of prothrombin to thrombin, a key regulatory enzyme in the formation of a blood clot. Interestingly, a virtually identical enzyme complex is found in the venom
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The macromolecular enzyme complex prothrombinase serves an indispensable role in blood coagulation as it catalyzes the conversion of prothrombin to thrombin, a key regulatory enzyme in the formation of a blood clot. Interestingly, a virtually identical enzyme complex is found in the venom of some Australian elapid snakes, which is composed of a cofactor factor Va-component and a serine protease factor Xa-like subunit. This review will provide an overview of the identification and characterization of the venom prothrombinase complex and will discuss the rationale for its powerful procoagulant nature responsible for the potent hemostatic toxicity of the elapid venom. Full article
(This article belongs to the Special Issue Protein Toxins as Proteases)
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