Abstract
The coagulant protein has been obtained from Russell''s-viper venom as a physically homogeneous component with a specific activity eight times that of the crude venom. The coagulant protein functions as an enzyme in activating a coagulation factor present in bovine serum, and catalyses the hydrolysis of a synthetic proteinase substrate, toluene-p-sulphonylarginine methyl ester. Toluene-p-sulphonylarginine methyl ester functions as a competitive inhibitor of the activation of a coagulation factor in bovine serum by the purified coagulant protein.