Literature DB >> 1148215

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

G O'Cuinn, P F Fottrell.   

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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Year:  1975        PMID: 1148215     DOI: 10.1016/0005-2744(75)90262-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Identifying the structure of the active sites of human recombinant prolidase.

Authors:  Roberta Besio; Stefania Alleva; Antonella Forlino; Anna Lupi; Carlo Meneghini; Velia Minicozzi; Antonella Profumo; Francesco Stellato; Ruggero Tenni; Silvia Morante
Journal:  Eur Biophys J       Date:  2009-05-05       Impact factor: 1.733

2.  Purification and characterization of a prolidase from Lactobacillus casei subsp. casei IFPL 731.

Authors:  M D Fernández-Esplá; M C Martín-Hernández; P F Fox
Journal:  Appl Environ Microbiol       Date:  1997-01       Impact factor: 4.792

3.  Intestinal peptide transport and hydrolysis in health and disease.

Authors:  P F Fottrell
Journal:  Ir J Med Sci       Date:  1979-12       Impact factor: 1.568

  3 in total

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