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.
Tanizaki
M M
MM
Serviço de Bioquímica, Instituto Butantan, São Paulo, Brasil.
Zingali
R B
RB
Kawazaki
H
H
Imajoh
S
S
Yamazaki
S
S
Suzuki
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003435:Crotalid Venoms / Q000032:analysis*; D004789:Enzyme Activation; D008666:Metalloendopeptidases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D008670:Metals / Q000032:analysis; D008969:Molecular Sequence Data; D015032:Zinc / Q000378:metabolism*
D003435:Crotalid Venoms; D008670:Metals; D008666:Metalloendopeptidases; D015032:Zinc