Purification and Characterization of an Aminoacyl Proline Hydrolase from Guinea-pig Intestinal Mucosa

Overview

Journal Biochim Biophys Acta

Specialties Biochemistry
Biophysics

Date 1975 Jun 24

PMID 1148215

Citations 3

Authors

G OCuinn

P F Fottrell

Affiliations

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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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