Isolation and activation of factor X from camel plasma

This study presents the purification of a well-characterized activated FX from the camel plasma. Also, due to the unavailability of Russell viper venom, this study presents Cerastus cerastus viper venom as a new alternative activator of FX. Camel factor X was purified by barium ion precipitation, ion exchange and affinity chromatography columns and activated to FXa with venom from the viper Cerastus cerastus. The specific activity of FXa was found to be 699.3 units/mg protein. It turned out to be homogenous on both native PAGE and 12% SDS PAGE with a molecular weight of 59kDa. The molecular weights of the two heavy and light chains of camel FX were determined to be 42kDa and 17kDa respectively. The Km value was found to be 91μM of N-Benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide HCl. Soybean trypsin inhibitor was the most potent inhibitor of camel FXa. The activated Fx displayed its optimum activity at pH 7.4.