Abstract
The conversion mechanism of prothrombin into thrombin was studied with purified factors in the limited proteolysis system. The purified prothrombin was utilized for the reaction of conversion of prothrombin into thrombin by Russell's viper venom, and the molecular weights of products were determined as follows by SDS polyacrylamide disc electrophoresis: Peak I, 32, 000±500; Peak II, 62, 000±1, 000; Peak III, 28, 000±500. Peak I contained a thrombin activity. Peak II contained a prothrombin activity. Peak III was suggested to contain a degraded product of prothrombin.
