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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1982-5-21
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pubmed:abstractText |
To explore the nature of retinyl ester synthesis by liver microsomes, membranes prepared from rat or cat liver were incubated under various conditions with [3H] retinol dispersed in dimethyl sulfoxide. When [3H]retinol, buffer, and microsomes were incubated together (basal conditions), some [3H]retinol esterification was consistently observed. However, the rate of esterification could be increased 6- to 11-fold by addition of either palmitoyl-CoA (100 microM) or a fatty acyl CoA-generating system. To determine whether the fatty acid used to esterify [3H]retinol under basal conditions might be derived from an endogenous pool of fatty acyl-CoA associated with the microsomal preparation, microsomes were pretreated at pH 7.4 with 0.5 M hydroxylamine, a reagent that reacts with coenzyme A thioesters to form hydroxamates. This pretreatment reduced the basal reaction by 69%. However, hydroxylamine-treated microsomes still retained acyltransferase activity, as shown by a 24- to 40-fold increase in retinyl ester synthesis after addition of palmitoyl-CoA. When microsomes were incubated with both [3H]retinol and [14C]palmitoyl-CoA of known specific radioactivities, the ratio of 14C to 3H in newly synthesized retinyl palmitate was essentially equal to that of its putative substrates, indicating that [14C]palmitate did not undergo significant isotope dilution prior to acylation of [3H]retinol. These experiments provide direct evidence for retinol esterification catalyzed by a microsomal acyl-CoA:retinol acyltransferase and indirect evidence for a pool of fatty acyl-CoA in isolated liver microsomes that is available to react with [3H]retinol to form esterified retinol.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitates,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitoyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/Retinol O-Fatty-Acyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin A,
http://linkedlifedata.com/resource/pubmed/chemical/retinol palmitate
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2453-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7061433-Acyltransferases,
pubmed-meshheading:7061433-Animals,
pubmed-meshheading:7061433-Female,
pubmed-meshheading:7061433-Kinetics,
pubmed-meshheading:7061433-Male,
pubmed-meshheading:7061433-Microsomes, Liver,
pubmed-meshheading:7061433-Palmitates,
pubmed-meshheading:7061433-Palmitoyl Coenzyme A,
pubmed-meshheading:7061433-Progesterone,
pubmed-meshheading:7061433-Rats,
pubmed-meshheading:7061433-Rats, Inbred Strains,
pubmed-meshheading:7061433-Retinol O-Fatty-Acyltransferase,
pubmed-meshheading:7061433-Vitamin A
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pubmed:year |
1982
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pubmed:articleTitle |
Retinol esterification by rat liver microsomes. Evidence for a fatty acyl coenzyme A: retinol acyltransferase.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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