Fibrin(ogen)olytic and platelet modulating activity of a novel protease from the Echis multisquamatis snake venom

The variety of enzymes including serine proteases that possess activity have been discovered in different snake venoms. In our work the platelet modulating activity of a new protease from was shown that puri substrate following much slower hydrolysis of C-terminus offibrin(ogen)olytic and platelet modulatingfibrin(ogen)olytic and Echis multisquamatis snake venom was studied. Itfied enzyme cleaved the ВbR42-A43 bond of fibrinogen during first contact with thefibrinogen Aa-chain. Protease hydrolysed fi B clotting time and the clot formed from a mixture of nativebrin clot too, but at much slower rate and cleaved both C-terminus of Aa-chain and ВbR42-A43 bond ofb-chain simultaneously. Preincubation of fibrinogen with protease dramatically elongated thrombinfibrinogen and fibrinogen desВb(1e42)2 digested by plasmin much faster than a native cause changes in their shape and granularity, but it reduced platelets aggregation induced by ADP.fibrin clot. The protease did not activate platelets nor