Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM. Binds 1 zinc ion per subunit. Inhibited by EDTA and 2-mercaptoethanol. Inhibited by 1 mM zinc ion and to a lesser extent by 1 mM calcium ion. Optimum pH is 7.0 for dimethylcasein with a complete loss of activity above pH 11.0. Optimum temperature is 30-40 degrees Celsius with a complete loss of activity above 60 degrees Celsius. Monomer. Expressed by the venom gland. Has no activity toward laminin (PubMed:16139412). Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.