Antiplatelet and anti-proliferative action of disintegrin from Echis multisquamatis snake venom.

Aim: To purify the platelet aggregation inhibitor from Echis multisquamatis snake venom (PAIEM) and characterize its effect on platelet aggregation and HeLa cell proliferation.

Methods: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix assisted laser desorption/ionization time-of-flight (MALDI-TOF) were used for PAIEM identification. Platelet aggregation in the presence of PAIEM was studied on aggregometer Solar-AP2110.

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.