Snake venom serine protease that shows non-specific action on fibrinogen (PubMed:30145175). It preferentially degrades fibrinogen Aalpha (FGA), releasing fibrinopeptide A, and shows a lower activity on fibrinogen Bbeta (FGB), releasing fibrinopeptide B and other uncommon fibrinopeptides (PubMed:30145175). Also shows low fibrinolytic activity compared to plasmin (PubMed:30145175). Has high enzymatic activity on the substrates for activated protein C and factor XIa, and for thrombin (PubMed:30145175). Shows a wide activity spectrum at different peptide sequences, with a preferential cleavage at Lys-|-Xaa over Arg-|-Xaa bonds (PubMed:30145175). Inhibited by benzamidine, PMSF, leupeptin, SDS and DTT, but not by EDTA, and commercial antivenom. Optimum pH is 7.5. Optimum temperature is 50 degrees Celsius. Monomer. Expressed by the venom gland. This protein seems to be found in adult B.jararaca venom but not in newborn snake venom. N-glycosylated. Contains approximately 10% carbohydrates. Does not cleave fibrinogen gamma chain (FGG) (PubMed:30145175). Does not form fibrin clots from fibrinogen solutions (PubMed:30145175). Has no effect on aggregation of washed platelets (PubMed:30145175). Has minor effects on the substrate for plasma kallikrein, plasmin and factor Xa, and also on certain isolated factors, such as prothrombin, factor X and protein C, not inducing the formation of their activated forms (PubMed:30145175). Also shows a very weak inhibitory activity on the human voltage-gated potassium channel Kv10.1/KCNH1/EAG1 (9.2% current inhibition at 5 uM) (PubMed:32161292). Belongs to the peptidase S1 family. Snake venom subfamily.