batroxobin

Batroxobin is a serine protease enzyme derived from the venom of the snake Bothrops moojeni (and also Bothrops atrox), classified as a thrombin-like enzyme. It acts as a defibrinogenating agent by specifically cleaving the 16 Arginine–17 Glycine bond in the A alpha chain of fibrinogen, releasing fibrinopeptide A and forming fibrin monomers that aggregate into clots. Unlike thrombin, batroxobin only splits off fibrinopeptide A and is not inhibited by antithrombin or heparin cofactor II. Its main clinical effects include reducing plasma fibrinogen levels, promoting clot formation, decreasing blood viscosity, improving microcirculation, and inducing endogenous tissue plasminogen activator (tPA) release from endothelial cells to promote thrombolysis. Batroxobin has been used experimentally for hemostasis after surgery and investigated for treatment of deep vein thrombosis, cerebral infarction, cerebral venous thrombosis (CVT), and other thrombotic diseases[1][2][4][5][6].

Brand names

Defibrase

Other names

fibrinolytic enzyme from snake venombatroxobinreptilase