title: Isolation of the prothrombin-converting enzyme from fibrinogenolytic enzymes of Echis carinatus venom by chromatographic and electrophoretic methods.
abstract: 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.
mesh_terms: D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D014757:Viper Venoms / Q000032:analysis*
chemical_list: D014757:Viper Venoms; D010450:Endopeptidases; C020097:ecarin