title: [Isolation and characteristics of the protein C activator from Agkistrodon halys halys snake venom].
abstract: Protein C activator from Agkistrodon halys halys venom has been isolated and purified by ion-exchange and gel-filtration chromatography. The purified enzyme consists of the single peptide-chain with molecular weight of 34 kDa. Its pH-optimum was in 7.5-8.0 range. The enzyme was inhibited by DFP, benzamidine, PMSF, EGTA. Protein C activator was as effective as "Protac" (Pentapharm AG, Switzerland).
authors.forename: T N
authors.initials: TN
authors.lastname: Platonova
authors.forename: O V
authors.initials: OV
authors.lastname: Gornitskaia
mesh_terms: D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry*; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D010314:Partial Thromboplastin Time; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000302:isolation & purification*; D011480:Protease Inhibitors / Q000494:pharmacology; D011486:Protein C / Q000032:analysis*; D013379:Substrate Specificity; D013927:Thrombosis / Q000097:blood / Q000517:prevention & control
chemical_list: C031442:Agkistrodon venoms; D003435:Crotalid Venoms; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D011480:Protease Inhibitors; D011486:Protein C; C049647:snake venom protein C activator; D010447:Peptide Hydrolases