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Coagulant serine proteinase (VLCII) was purified from <jats:italic>Vipera lebetina<\/jats:italic> venom using three chromatographic steps: gel filtration on SephadexG\u201075, DEAE\u2010Sephadex A\u201050, and reversed\u2010phase high\u2010performance liquid chromatography (RP\u2010HPLC) on C8 column. VLCII appeared homogenous (60 kDa) when tested on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS\u2010PAGE). VLCII as a thrombin\u2010like enzyme was able to hydrolyze N\u03b1\u2010CBZ L\u2010arginine\u2010p\u2010nitroanilide hydrochloride and could be a serine protease because it is inhibited by phenylmethylsulfonyl fluoride. The proteolytic activity of VLCII was not affected by ethylenediaminetetraacetic acid and 1.10\u2010phenanthroline. It showed high coagulant activity against human plasma and cleaved both A\u03b1 chain and B\u03b2 chain of bovine fibrinogen. The isolated VLCII displayed proaggregating effect on human platelet in a concentration\u2010dependent manner with an absence of lag time. Clopidogrel P2Y12 adenosine diphosphate (ADP) receptor inhibitor reduced markedly the aggregating effect induced by VLCII than aspirin, indicating the involvement of ADP signaling pathway.<\/jats:p>","DOI":"10.1002\/jbt.21709","type":"journal-article","created":{"date-parts":[[2015,4,28]],"date-time":"2015-04-28T07:23:55Z","timestamp":1430205835000},"page":"388-397","source":"Crossref","is-referenced-by-count":7,"title":["Purification and Characterization of a New Serine Protease (VLCII) Isolated from <i>Vipera lebetina<\/i> Venom: Its Role in Hemostasis"],"prefix":"10.1002","volume":"29","author":[{"given":"Kadi\u2010Saci","family":"Amel","sequence":"first","affiliation":[{"name":"USTHB, Faculty of Biological Sciences Laboratory of Cellular and Molecular Biology  BP32 El\u2010Alia Bab Ezzouar Algiers Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laraba\u2010Djebari","family":"Fatima","sequence":"additional","affiliation":[{"name":"USTHB, Faculty of 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