Document Detail

Purification and some properties of a medium-chain acyl-thioester hydrolase from lactating-rabbit mammary gland which terminates chain elongation in fatty acid synthesis.
MedLine Citation:
PMID:  1035109     Owner:  NLM     Status:  MEDLINE    
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.
J Knudsen; S Clark; R Dils
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  160     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1976 Dec 
Date Detail:
Created Date:  1977-03-21     Completed Date:  1977-03-21     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  683-91     Citation Subset:  IM    
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MeSH Terms
Albumins / pharmacology
Coenzyme A / metabolism
Fatty Acids / biosynthesis*
Hydrolases / metabolism
Mammary Glands, Animal / enzymology*
Molecular Weight
Thiolester Hydrolases / isolation & purification*
Reg. No./Substance:
0/Albumins; 0/Fatty Acids; 85-61-0/Coenzyme A; EC 3.-/Hydrolases; EC 3.1.2.-/Thiolester Hydrolases

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

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