Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity.

摘要: Abstract Our studies of the venom from Levantine viper Vipera lebetina have demonstrated existence both coagulants and anticoagulants hemostatic system in same venom. We showed that V. contains factor X activator (VLFXA) V activator, fibrinolytic enzymes. VLFXA was separated by gel filtration on Sephadex G-100 superfine ion exchange chromatography CM-cellulose TSK-DEAE (for HPLC) columns. is a glycoprotein composed heavy chain (57.5 kDa) two light chains (17.4 kDa 14.5 linked disulfide bonds. has multiple molecular forms distinguished their isoelectric points. The differences pI values may be caused dissimilarities respective charged carbohydrate content or primary sequence amino acids. synthesized 6–9 acid residues containing peptides according to physiological cleavage regions human IX. (Asn-Asn-Leu-Thr-Arg-Ile-Val-Gly-Gly – fragment, Asn-Asp-Phe-Thr-Arg-Val-Val-Gly-Gly IX fragment) were used as substrates for direct assay VLFXA. Cleavage products peptide hydrolysis masses determined MALDI-TOF MS. MS highly efficient recovery identification released hydrolysis. can conclude cleaves Arg52-Ile53 bond Arg226-Val227 precursor. could not activate prothrombin nor had any effect fibrinogen, it no arginine esterase activity toward benzoylarginine ethyl ester.