title: Biochemical characterization of fibrinogenolytic serine proteinases from Vipera lebetina snake venom.
abstract: Two glycosylated serine fibrinogenases isolated from Vipera lebetina venom have homologous N-terminal sequences and antigenic determinants but can be clearly differentiated according to substrate specificity, glycosylation levels, molecular mass and fibrinogen degradation. alpha-Fibrinogenase has no homolog among known serine proteinases. It has N-terminal similarity with snake venom arginine esterases but does not hydrolyze the esters of arginine, lysine and tyrosine. The enzyme has strong proteolytic activity and degrades alpha-chain of fibrinogen altering its clottability by thrombin. beta-Fibrinogenase is a typical arginine esterase which hydrolyzes esters and amides of arginine and attacks the beta-chain of fibrinogen.
authors.affiliation: National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618, Tallinn, Estonia.
authors.forename: Mari
authors.initials: M
authors.lastname: Samel
authors.forename: Juhan
authors.initials: J
authors.lastname: Subbi
authors.forename: Jüri
authors.initials: J
authors.lastname: Siigur
authors.forename: Ene
authors.initials: E
authors.lastname: Siigur
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000276:immunology / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism; D005343:Fibrinolytic Agents / Q000276:immunology / Q000378:metabolism*; D006031:Glycosylation; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000276:immunology / Q000378:metabolism*; D013379:Substrate Specificity; D014757:Viper Venoms / Q000201:enzymology* / Q000276:immunology; D017819:Viperidae / Q000502:physiology*
chemical_list: D005343:Fibrinolytic Agents; D014757:Viper Venoms; D005340:Fibrinogen; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases; D012697:Serine Endopeptidases