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. 1975 Jun 24;391(2):388-95.
doi: 10.1016/0005-2744(75)90262-4.

Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa

Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa

G O'Cuinn et al. Biochim Biophys Acta. .

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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