Isolation and characterization of a new aminopeptidase from bovine lens.
作者： B J Ortwerth , K K Sharma
DOI: 10.1016/S0021-9258(17)35660-0
关键词:
摘要: An aminopeptidase has been purified to homogeneity from bovine lens tissue by gel filtration and DEAE-cellulose chromatography. This enzyme a molecular weight of 96,000 under both native denaturing conditions. The hydrolyzed variety synthetic substrates as well di-, tri-, higher peptides. Significantly this is capable hydrolyzing arginine, lysine, proline aminoacyl bonds. pH optimum for activity stability was 6.0. Both reduced sulfhydryl group divalent metal ion are essential activity. contains 1.6 mol zinc 1.0 copper/mol enzyme. No activation seen upon incubation with either magnesium or manganese; however, heavy ions were inhibitory. Bestatin puromycin effective inhibitors no endopeptidase could be detected in the preparation. clearly distinct leucine aminopeptidase, but rather, identical cytosolic III isolated other tissues. Evidence presented which argues that may major vivo
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