Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa
- PMID: 1148215
- DOI: 10.1016/0005-2744(75)90262-4
Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa
Abstract
The purification of an aminoacylproline hydrolase from guinea-pig intestinal mucosa is described. The enzyme, which is an aminopeptidase has a molecular weight of 112 000 and is activated by manganese and inhibited by zinc. Unlike other aminoacylproline hydrolases this enzyme displayed a broad substrate specificity. However, it was preferentially active against dipeptides containing proline in the C-terminal position.
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