Document Detail


Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys.
MedLine Citation:
PMID:  4038259     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Carboxypeptidase P has been purified by immunoaffinity chromatography from pig kidneys. A single-step assay with Z-Pro-Met (where Z represents benzyloxycarbonyl) as substrate was used, methionine being determined by using L-amino acid oxidase and horseradish peroxidase. The enzyme constitutes about 1.5% of the kidney microvillar proteins. Triton X-100-solubilized and papain-released forms of the enzyme were isolated. The former had an apparent subunit Mr of 135 000, and the latter form contained two polypeptide chains of Mr 128 000 and 95 000. The undenatured forms were dimeric proteins. In common with other microvillar hydrolases, carboxypeptidase P was a glycoprotein and each subunit contained one Zn atom. MnCl2 (1 mM) in the assay was necessary for maximum activity; in its absence, 0.5 mM-ZnSO4 produced a limited activation, but was inhibitory at higher concentrations. The Km for Z-Pro-Met, in the presence of MnCl2, was 4.1 mM, and the kcat. for freshly prepared enzyme was 1230 min-1. The enzyme lost activity during storage at -20 degrees C. In a limited survey of peptides, hydrolysis was observed only with substrates containing a proline, alanine or glycine residue in the P1 position, and these included angiotensins II and III. The best substrate in this series was Val-Ala-Ala-Phe.
Authors:
S Hedeager-Sørensen; A J Kenny
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  229     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1985 Jul 
Date Detail:
Created Date:  1985-09-27     Completed Date:  1985-09-27     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  251-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Carboxypeptidases / isolation & purification,  metabolism*
Cations, Divalent / pharmacology
Electrophoresis, Polyacrylamide Gel
Hydrolysis
Kidney Cortex / enzymology*
Kinetics
Microvilli / enzymology
Molecular Weight
Peptides / metabolism
Swine
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Cations, Divalent; 0/Peptides; EC 3.4./carboxypeptidase P; EC 3.4.-/Carboxypeptidases
Comments/Corrections

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