Snake venom serine protease that has a potent and selective fibrinogenolytic activity. Preferentially cleaves the alpha-chain (FGA) of human and rat fibrinogen at Arg-|-Gly bonds, and slowly digests the beta-chain (FGB) (PubMed:18433459). In vivo, completely avoids thrombus formation induced in rat, decreases the fibrinogen plasma level and prolonges the recalcification time. Possesses esterolytic and amidolytic activities. Inhibited by diisopropylfluorophosphate (DFP), but not by SBTI, Antithrombin III/heparin and BPTI, probably due to steric hindrance caused by its huge carbohydrate moietie. Optimum pH is 3-9. Thermostable. Monomer. Expressed by the venom gland. N- and O-glycosylated. The glycosylation has a stabilizing effect on the protein (PubMed:14580991). However, the removal of part of the carbohydrates enhances the proteolytic activity of the SVSP towards human and rat fibrinogen (PubMed:18433459). Does not have coagulant activities and does not cause unspecific degradation of plasma proteins. Does not degrade gamma chain of fibrinogen (FGG) and is not active towards fibrin clots. Belongs to the peptidase S1 family. Snake venom subfamily.