Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis.
A simple procedure, involving chromatography on concanavalin A-Sepharose and gel filtration, has been developed for the purification of a prothrombin activator from the venom of the Australian brown snake Pseudonaja textilis textilis. The prothrombin activator, which is a major venom component, is a high molecular weight protein (Mr greater than or equal to 200,000) which yields a number of subunits when examined by SDS-PAGE. It is related antigenically to the venom prothrombin activator of the taipan Oxyuranus scutellatus. P. textilis prothrombin activator is able to coagulate citrated plasma, warfarin plasma, and Factor V- and Factor X-deficient plasmas; to convert purified human prothrombin to thrombin; and to hydrolyse the peptide p-nitroanilide substrate S-2222. Calcium ions and phospholipids had little if any effect on the rates of coagulation of citrated plasma or S-2222 hydrolysis catalysed by this enzyme.
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Department of Medicine, University of Queensland, Princess Alexandra Hospital, Woolloongabba, Australia.
Whitaker
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de Jersey
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D000818:Animals; D001315:Australia; D001780:Blood Coagulation Tests; D002384:Catalysis; D002850:Chromatography, Gel; D003208:Concanavalin A; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011516:Prothrombin / Q000378:metabolism*; D012685:Sepharose; D012910:Snake Venoms / Q000032:analysis*
D012910:Snake Venoms; D003208:Concanavalin A; D011516:Prothrombin; D012685:Sepharose; D010447:Peptide Hydrolases