Snake venom zinc metalloprotease that has fibrinogenolytic and hemorrhagic activities in mouse and rats. Hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain of fibrinogen (FGB), without affecting the gamma-chain. Its hemorrhagic activity results of its involvement in cleavage of basal membrane components (nidogen and fibronectin but not laminin) and depletion of fibrinogen, prothrombin (F2) and factor X (F10) in blood circulation. Also possess potent azocaseinolytic activity and cleaves insulin B-chain, hydrolyzing it at positions Gln(4)-His(5), His(10)-Leu(11) and Tyr(16)-Leu(17). Binds 1 zinc ion per subunit. Inhibited by EDTA, DTT and zinc ions. Partially inhibited by L-cysteine. Not inhibited by 2-propanol or PMSF. Activity is enhanced by calcium or magnesium ions. Heterodimer; disulfide-linked. Expressed by the venom gland. The N-terminus is blocked. N-glycosylated. Monomer. The hemorrhagic activity of the whole venom is completely neutralized by an antiserum against this metalloproteinase. Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIc sub-subfamily.