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 fibrin(ogen)olytic and platelet modulating activity have been discovered in different snake venoms. In our work the fibrin(ogen)olytic and platelet modulating activity of a new protease from Echis multisquamatis snake venom was studied. It was shown that purified enzyme cleaved the ВβR42-A43 bond of fibrinogen during first contact with the substrate following much slower hydrolysis of C-terminus of fibrinogen Aα-chain. Protease hydrolysed fibrin clot too, but at much slower rate and cleaved both C-terminus of Aα-chain and ВβR42-A43 bond of Bβ-chain simultaneously. Preincubation of fibrinogen with protease dramatically elongated thrombin clotting time and the clot formed from a mixture of native fibrinogen and fibrinogen desВβ(1-42)2 digested by plasmin much faster than a native fibrin clot. The protease did not activate platelets nor cause changes in their shape and granularity, but it reduced platelets aggregation induced by ADP.