Purification and Properties of Bradykininogen and of the Bradykinin-Releasing and -Destroying Enzymes in Snake Venom

Abstract

The arginine ester hydrolase in the venom of Agkistrodon halys blomhoffii (“Mamushi” in Japanese) was separated into three enzymatic entities: the “bradykinin-releasing,” “clotting,” and “capillary permeability-increasing” enzymes. The latter two enzymes were purified to physicochemically homogeneous states (Sato et al., 1965), and the bradykinin-releasing enzyme described in this paper containedno “clotting” or “capillary permeability-increasing” enzyme, and no bradykinin-destroying enzyme. The properties of the bradykinin-releasing enzyme of the venom were similar to those of pancreatic kallikrein (Werle and Trautschold, 1963). The authors also purified bovine bradykininogen, and from the results of Sanger’s DNP method, exopeptidase digestion methods, and the release of bradykinin by the venom bradykinin-releasing enzyme, it was concluded that bradykinin is not located at either end of the polypeptide chain of bradykininogen.