| Purification and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis. | |
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MedLine Citation:
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PMID: 1035109 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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1. An acyl-thioester hydrolase was isolated from the cytosol of lactating-rabbit mammary gland. The purified enzyme terminates fatty acid synthesis at medium-chain (C8:0-C12:0) acids when it is incubated with fatty acid synthetase and rate-limiting concentrations of malonyl-CoA. These acids are characteristic products of the lactating gland. 2. The mol.wt. of the enzyme is 29000+/-500 (mean+/-S.D. of three independent preparations), as estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 3. The enzyme also hydrolyses acyl-CoA esters of chain lengths C10:0-C16:0 when these are used as model substrates. The greatest activity was towards dodecanoyl-CoA, and the three preparations had specific activities of 305, 1130 and 2010 nmol of dodecanoyl-CoA hydrolysed/min per mg of protein when 56muM substrate was used. 4. The way in which this enzyme controls the synthesis of medium-chain fatty acids by fatty acid synthetase is briefly discussed. |
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Authors:
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J Knudsen; S Clark; R Dils |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: The Biochemical journal Volume: 160 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 1976 Dec |
Date Detail:
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Created Date: 1977-03-21 Completed Date: 1977-03-21 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 683-91 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Albumins
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pharmacology Animals Coenzyme A / metabolism Fatty Acids / biosynthesis* Female Hydrolases / metabolism Lactation* Mammary Glands, Animal / enzymology* Molecular Weight Pregnancy Rabbits Thiolester Hydrolases / isolation & purification* |
| Chemical | |
Reg. No./Substance:
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0/Albumins; 0/Fatty Acids; 85-61-0/Coenzyme A; EC 3.-/Hydrolases; EC 3.1.2.-/Thiolester Hydrolases |
| Comments/Corrections | |
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