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

Volodymyr Chernyshenko, Tetyana Platonova, Yevgen Makogonenko, Andriy Rebriev, Lyuba Mikhalovska, Tamara Chernyshenko, Serhiy Komisarenko

Research output: Contribution to journalArticle

Abstract

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
Original languageEnglish
Pages (from-to)76-83
Number of pages8
JournalBiochimie
Volume105
DOIs
Publication statusPublished - 31 Oct 2014

Keywords

  • Fibrinogenase
  • Fibrinogen
  • Platelet aggregation
  • Fibrin polymerization
  • Snake venom

Fingerprint Dive into the research topics of 'Fibrin(ogen)olytic and platelet modulating activity of a novel protease from the Echis multisquamatis snake venom'. Together they form a unique fingerprint.

Cite this