Non-hemorrhagic snake venom zinc metalloprotease that hydrolyzes the Aalpha-chain of fibrinogen, more slowly the Bbeta-chain and shows no effect on the gamma chain. Has no coagulant activity on bovine plasma and fibrinogen. Binds 1 zinc ion per subunit. Inhibited by EDTA, 1,10-phenanthroline and beta-mercaptoethanol. Not inhibited by the serine protease inhibitors aprotinin and benzamidin. Highest activity at neutral to basic pH. Reduced activity at pH 3.0. Activity is highest at 4 degrees Celsius, decreases with increasing temperatures and is lost at 60 degrees Celsius. Monomer. Expressed by the venom gland. Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.