| Glutathione-dependent fatty acylprotein deacylase. | |
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MedLine Citation:
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PMID: 1799363 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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S A Ibrahim; K A Balasubramanian |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemistry international Volume: 24 ISSN: 0158-5231 ISO Abbreviation: Biochem. Int. Publication Date: 1991 Jul |
Date Detail:
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Created Date: 1992-04-13 Completed Date: 1992-04-13 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8100311 Medline TA: Biochem Int Country: AUSTRALIA |
Other Details:
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Languages: eng Pagination: 595-604 Citation Subset: IM |
Affiliation:
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Wellcome Research Unit, Christian Medical College Hospital, Vellore, India. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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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:
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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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