概述

Thrombin is a "trypsin-like" serine protease protein. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the stemming of blood loss. As a result of cleaving, thrombin has two chains: a light chain (A chain, MW ~6 kDa) and a heavy chain (B chain, MW ~31 kDa). These two chains are joined by one disulfide bond. Functions of thrombin are that it converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzes many other coagulation-related reactions. Thrombin also contains g-carboxyglutamyl residues. These modified glutamyl residues are the result of carboxylation by a microsomal enzyme, vitamin Kdependent carboxylase. g-Carboxyglutamyl residues are necessary for the Ca2+-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.

使用說(shuō)明

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