Purification and some characteristics of a zinc metalloprotease from the venom of Bothrops jararaca (jararaca).

A metalloprotease from Bothrops jararaca venom (J protease) was purified by DEAE-Sephacel, CM-cellulose, Sephacryl S-200 and Sephadex G-75 chromatograph. The proteolytic activity was inactivated by EDTA, o-phenanthroline and DTNB. Phosphoramidon and cysteine protease inhibitors (leupeptin, E64 and its derivatives) were inactive on this enzyme. J protease was activated by calcium and the metal content analysis showed the presence of one mole each of tightly bond zinc and calcium per mole of this J protease. The amino acid composition, N-terminal amino acid sequence (29 residues) and the cleavage sites on the oxidized insulin B chain and angiotensin I were determined.