Snake venom serine protease active on several blood coagulation enzymes. It completely cleaves fibrinogen Aalpha chain (FGA) after 120 minutes, partially cleaves Bbeta chain (FGB) (overnight) and has no activity on gamma chain. It does not release fibrinopeptides A and/or B exclusively, since the enzyme does not provoke fibrin polymerisation. It also degrades fibrin as efficiently as plasmin, and exhibits potent ability to cleave plasminogen and prothrombin, as well as heavy chain of factor X (F10). In vitro, it cleaves insulin B-chain (at positions His38-Leu39, Ala40-Leu41 and Tyr16-Leu17). Inhibited by Pefabloc (90% inhibition), DTT (90%), Zn(2+) (80%), trypsin inhibitor II (50%), and benzamidine (45%), but not inhibited by EDTA, Ca(2+), Mg(2+) AND L-Cys. Optimum pH is 9.0. Monomer. Expressed by the venom gland. N-glycosylated. The protein exist in multiple isoforms. Belongs to the peptidase S1 family. Snake venom subfamily. Contains two of the three conventional residues of the catalytic triad: Asp and Ser are conserved, whereas the conventional His is replaced by an Arg. Residues 23 to 200 are identified by mass spectrometry.