Snake venom zinc metalloprotease that is weakly hemorrhagic and has Aalpha, Bbeta fibrinogenolytic activities. Cleaves the Aalpha chain of fibrinogen first, followed by the Bbeta chain and shows no effect on the gamma chain. Has caseinolytic activity. Induces dose-dependent edema. Binds 1 zinc ion per subunit. Inhibited by EDTA and EGTA. Inhibited by serum and antihemorrhagic factors Da2-I and Da2-II from D.albiventris. Not inhibited by PMSF or SBT-I. Optimum pH is 8. Activity decreases rapidly at higher or lower pH. Optimum temperature for caseinolytic activity is 40 degrees Celsius. Activity decreases rapidly at higher or lower temperatures. No activity below 10 degrees Celsius or above 70 degrees Celsius. Monomer. Expressed by the venom gland. Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.