[Isolation and characterization of a protein C activator from the moccasin snake venom].
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.
Storozhilova
A N
AN
Smirnov
M D
MD
Dobrovol'skiĭ
A B
AB
Kudriavtsev
S V
SV
Titov
V N
VN
D000818:Animals; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D008970:Molecular Weight; D011486:Protein C
D003435:Crotalid Venoms; D011486:Protein C
Vydelenie i kharakteristika aktivatora proteina C iz iada mokassinovogo shchitomordnika.