Document Detail


Glutathione-dependent fatty acylprotein deacylase.
MedLine Citation:
PMID:  1799363     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Monkey intestinal brush border membrane (BBM) when incubated with reduced glutathione (GSH), was found to release covalently bound fatty acids. However this activity was greatly reduced with delipidated BBM and nonexistent with heat-treated BBM. This release was specific for GSH since other thiol compounds such as DTT, cysteine, or oxidized glutathione could not do so. There was a concentration-dependent increase in deacylation with increasing concentration of GSH. Deacylation was pH dependent, and maximum activity was seen at pH 7.5. These results indicate that possibly a glutathione-dependent enzyme is involved in deacylation of membrane proteins and this may have a role in the turnover of fatty acid-acylated proteins.
Authors:
S A Ibrahim; K A Balasubramanian
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry international     Volume:  24     ISSN:  0158-5231     ISO Abbreviation:  Biochem. Int.     Publication Date:  1991 Jul 
Date Detail:
Created Date:  1992-04-13     Completed Date:  1992-04-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8100311     Medline TA:  Biochem Int     Country:  AUSTRALIA    
Other Details:
Languages:  eng     Pagination:  595-604     Citation Subset:  IM    
Affiliation:
Wellcome Research Unit, Christian Medical College Hospital, Vellore, India.
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MeSH Terms
Descriptor/Qualifier:
Acylation
Animals
Endopeptidases / metabolism
Esterases / metabolism*
Fatty Acids / metabolism*
Glutathione / metabolism*
Intestine, Small / enzymology*,  ultrastructure
Macaca radiata
Membrane Proteins / metabolism
Microvilli / enzymology,  metabolism
Protein Processing, Post-Translational
Sulfhydryl Compounds / pharmacology
Chemical
Reg. No./Substance:
0/Fatty Acids; 0/Membrane Proteins; 0/Sulfhydryl Compounds; 70-18-8/Glutathione; EC 3.1.-/Esterases; EC 3.4.-/Endopeptidases

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


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