Isolation of the prothrombin-converting enzyme from fibrinogenolytic enzymes of Echis carinatus venom by chromatographic and electrophoretic methods.
Chromatography of crude Echis carinatus venom revealed four enzymes with fibrinogenolytic activity and activity to chromogenic substrates, specific for proteases of the coagulation and fibrinogenolytic systems. By employing three-step chromatography on DEAE-Sephacel and Sephacryl S-200, this venom afforded the procoagulation enzyme Ecarin in good recovery (73%) and purification (53-fold). This highly purified preparation has proved to be a single-chain glycoprotein, occurring in two isomers differing in electrical charge and having a low fibrinogenolytic activity.
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D014757:Viper Venoms / Q000032:analysis*
D014757:Viper Venoms; D010450:Endopeptidases; C020097:ecarin