Abstract

Snake venom prothrombin activators have been shown to be excellent tools in diagnostic coagulation assays and in studying the mechanism of prothrombin activation. In this review we give an historical overview of the discovery of snake venom prothrombin activators and of their mechanisms of action on prothrombin. Based on the effects of the accessory components of the human prothrombin-activating complex (calcium ions, phospholipids and factor Va), venom prothrombin activators can be divided into four groups comprising activators that are metalloproteinases which either do not require accessory components (group A) or which require calcium ions for expressing activity (group B). The other activators are serine proteases that share homology with blood coagulation factor Xa and which require phospholipids plus calcium ions for optimal activity (Group C) or the activity of which is greatly enhanced by calcium ions, phospholipids and factor Va (group D).

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