A new fibrinogenase from Echis multisquamatis venom is a perspective agent for limited proteolysis and defibrinogenation

A serine proteinase with a fibrinogenase activity was isolated from the venom of viper Echis multisquamatis. Isolation was performed by the combination of Q-sepharose and Heparine-agarose chromatography. The enzyme has apparent molecular weight 35 +/- 1 kDa. It posesses strong fibrinogen beta -chain, moderate alpha -chain proteolytic activity, arginine-amidase activity as the majority of serine fibrinogenases. The Km value was determined for beta -chain fibrinogenolytic activity: Km = 8.3 mu M. Kinetic parameters for amidase activity were also determined. Amino-acid composition was revealed. Limited hydrolysis of fibrinogen by the obtained fibrinogenase allowed us to detemine stable hydrolytic subproducts with definite molecular weights. The manner of the proteolytic processes suggests possible use of this fibrinogenase in probing fibrinogen structure dinamics by limited proteolysis. Applicability of the obtained fibrinogenase in therapeutic practice is speculative, but presented data about its nature are encouraging and require additional investigation.