Isolation and properties of a T-kininogenase from bovine erythrocyte membranes.
A kininogenase from bovine erythrocyte membranes has been purified 140-fold by affinity chromatography on pepstatin A-Agarose followed by ion exchange chromatography on CM Cellulose. The purified enzyme showed an apparent molecular weight of 31,000 daltons as measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its pH optimum is 7.5, and it was totally inhibited by soybean trypsin inhibitor, phenylmethyl-sulfonylfluoride, aprotinin, pepstatin, and dithiotreitol, suggesting the presence of a disulfide bond(s) whose integrity is(are) essential for maintaining the native three-dimensional structure. The referred enzyme was able to release kinin from a substrate partially purified from rat plasma. The kininogenase was activated by Zn2+, Ca2+, and cysteine-HCl.
Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, Brazil.
L A
LA
Ferreira
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M
Bergamasco
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Henriques
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004910:Erythrocyte Membrane / Q000201:enzymology*; D005260:Female; D006168:Guinea Pigs; D007610:Kallikreins / Q000737:chemistry / Q000302:isolation & purification*; D008297:Male; D008969:Molecular Sequence Data; D051381:Rats; D017208:Rats, Wistar
D007610:Kallikreins