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Toxins 2010, 2(6), 1554-1567; doi:10.3390/toxins2061554
Review

Procoagulant Adaptation of a Blood Coagulation Prothrombinase-like Enzyme Complex in Australian Elapid Venom

1
 and 1,2,*
1 Department of Pediatrics, Division of Hematology, The Children’s Hospital of Philadelphia, Philadelphia, PA 19104, USA 2 The University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA
* Author to whom correspondence should be addressed.
Received: 30 March 2010 / Revised: 4 June 2010 / Accepted: 17 June 2010 / Published: 18 June 2010
(This article belongs to the Special Issue Protein Toxins as Proteases)
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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 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.
Keywords: snake venom; blood coagulation; prothrombinase complex; factor X; factor V; prothrombin activation; serine protease; hemostatic toxin snake venom; blood coagulation; prothrombinase complex; factor X; factor V; prothrombin activation; serine protease; hemostatic toxin
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Bos, M.H.; Camire, R.M. Procoagulant Adaptation of a Blood Coagulation Prothrombinase-like Enzyme Complex in Australian Elapid Venom. Toxins 2010, 2, 1554-1567.

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