title: [Isolation and characterization of a protein C activator from the moccasin snake venom].
abstract: The protein C activator detectable in the venom of the Southern Copperhead snake (Agkistrodon contortrix contortrix) was isolated by a combination of chromatofocusing on PBE-94 in the range pH9-7 and gel-filtration on Sephadex G-100 column. The peak protein C activator from Sephadex G-100 column appeared as double diffuse bands with apparent molecular weight of 37,700 and 31,400 after electrophoresis in the presence of sodium dodecylsulfate and 2-mercaptoethanol. The isolated enzyme does not clot human fibrinogen and when mixed with normal plasma generates activity of Protein C. It can be used for the measurement of protein C functional activity.
authors: A N
authors: AN
authors: Storozhilova
authors: M D
authors: MD
authors: Smirnov
authors: A B
authors: AB
authors: Dobrovol'skiĭ
authors: S V
authors: SV
authors: Kudriavtsev
authors: V N
authors: VN
authors: Titov
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D008970:Molecular Weight; D011486:Protein C
chemical_list: D003435:Crotalid Venoms; D011486:Protein C
vernacular_title: Vydelenie i kharakteristika aktivatora proteina C iz iada mokassinovogo shchitomordnika.