Purification and characterization of an aminoacyl proline hydrolase from guinea-pig intestinal mucosa.
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.
D000818:Animals; D002413:Cations, Divalent; D002414:Cations, Monovalent; D002729:Chloromercuribenzoates / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D004150:Dipeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004592:Electrophoresis, Starch Gel; D006168:Guinea Pigs; D007413:Intestinal Mucosa / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D010618:Phenanthrolines / Q000494:pharmacology; D011392:Proline; D013329:Structure-Activity Relationship
D002413:Cations, Divalent; D002414:Cations, Monovalent; D002729:Chloromercuribenzoates; D010618:Phenanthrolines; D011392:Proline; D004150:Dipeptidases