Snake venom zinc metalloprotease that has Aalpha, Bbeta fibrin(ogen)olytic activities. It cleaves the Aalpha chain of fibrinogen first followed by the Bbeta chain and shows no effect on the gamma chain. Does not induce or inhibit platelet aggregation, and is unable to activate plasminogen. Exhibits low lethality when tested on mice. Intravenous administration results in thrombolysis within one hour followed by recanalization. Fibrinogenolytic activity results in a 60% decrease in the rat's plasma fibrinogen level. Histological examination of kidney, liver, heart and lung tissue shows no necrosis nor hemorrhage. Cleavage of 5-His-|-Leu-6, 9-Ser-|-His-10, 10-His-|-Leu-11, 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in insulin B chain. Binds 1 zinc ion per subunit. Inhibited by EDTA and alpha2-macroglobulin. Optimum pH is 9.0. Optimum temperature is 55 degrees Celsius. Monomer. Expressed by the venom gland. The N-terminus is blocked. Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.