Procoagulant activities in venoms from central Asian snakes.
The venoms from central Asian snakes (Echis carinatus, Echis multisquamatus, Vipera ursini, Vipera lebetina, Agkistrodon halys halys and Naja naja oxiana) contain several enzymes with amidolytic- and procoagulant activity. We have characterized the activities and the mol. wts of the venom enzymes that are able to convert a number of commercially available chromogenic substrates for activated coagulation factors. The chromogenic substrate cleavage patterns obtained for the crude venoms may be helpful tools in the further identification of venom fractions and venom enzymes with procoagulant activity. The crude venoms were also tested for their ability to clot fibrinogen, to lyse fibrin polymers and to activate the coagulation factors prothrombin, factor X and factor V. The products of venom-catalyzed coagulation factor activation were structurally characterized by SDS gel electrophoresis and were compared with activated coagulation factors that are generated under physiological conditions.
Yukelson
L Y
LY
Institute of Biochemistry of the Uzbek Academy of Sciences, Tashkent, U.S.S.R.
Tans
G
G
Thomassen
M C
MC
Hemker
H C
HC
Rosing
J
J
D000577:Amides / Q000378:metabolism*; D001777:Blood Coagulation / Q000187:drug effects*; D002384:Catalysis; D002863:Chromogenic Compounds / Q000378:metabolism; D005165:Factor V / Q000378:metabolism; D015943:Factor Va / Q000032:analysis; D005170:Factor X / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D011516:Prothrombin / Q000378:metabolism; D012910:Snake Venoms / Q000494:pharmacology*; D014610:Uzbekistan
D000577:Amides; D002863:Chromogenic Compounds; D012910:Snake Venoms; D015943:Factor Va; D005165:Factor V; D011516:Prothrombin; D005170:Factor X