Document Detail

Subcellular localisation of di- and tripeptidases in guinea pig and rat enterocytes.
MedLine Citation:
PMID:  465509     Owner:  NLM     Status:  MEDLINE    
Enterocytes were isolated from rat and guinea pig jejunum and subcellular fractions were prepared by density gradient centrifugation. Gradient fractions were assayed for principal organelle marker enzymes and for di- and tripeptidases. The hydrolases showed a dual localisation with both brush border and cytosol components. In the rat, approximately equal portions of dipeptidase activities were found in the two fractions but, in the guinea pig, three times more activity were found in the two fractions but, in the guinea pig, three times more activity was found in the soluble than in the brush border fractions. Cytosol components in the rat were markedly inhibited by p-hydroxymercuribenzoate. In both species tripeptidase, leucyl-2-naphthylamidases and gamma-glutamyltransferase activities were found predominantly in the brush border fractions.
G P Wells; J A Nicholson; T J Peters
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  569     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1979 Jul 
Date Detail:
Created Date:  1979-10-26     Completed Date:  1979-10-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  82-8     Citation Subset:  IM    
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MeSH Terms
Cell Fractionation
Centrifugation, Density Gradient
Dipeptidases / isolation & purification*
Guinea Pigs
Jejunum / enzymology*,  ultrastructure
Microvilli / enzymology
Mitochondria / enzymology
Peptide Hydrolases / isolation & purification*
Species Specificity
Reg. No./Substance:
0/Oligopeptides; EC 3.4.-/Peptide Hydrolases; EC 3.4.13.-/Dipeptidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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