Snake venom zinc metalloproteinase that cleaves the alpha chain of fibrinogen (FGA) first followed by the beta chain (FGB) and shows no effect on the gamma chain. Cleaves only the beta chain of fibrin, leaving the gamma-dimer untouched. Shows proteolytic activity towards azocasein. Causes defibrinogenation when intraperitoneally administered on mice. Binds 1 zinc ion per subunit. Inhibited by EDTA. Not inhibited by the serine proteinase inhibitors aprotinin and benzamidine. Optimum pH is 8.0. Monomer. Expressed by the venom gland. Is devoid of hemorrhagic, thrombin-like, and phospholipase A2 activities. Has no hemorrhagic activity in mice (PubMed:18187176). Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.