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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
1985-2-20
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| pubmed:abstractText |
Lignoceroyl-CoA ligase activity has been detected in microsomal fractions prepared from rat brain. The synthesis of lignoceroyl-CoA from [1-14C]lignoceric acid and CoASH by this enzyme had an absolute dependence on ATP and Mg2+; ATP could not be replaced by GTP [I. Singh, M. S. Kang, and L. Phillips (1982) Fed. Proc. 41, 1192]. The product has been characterized as lignoceroyl-CoA by the following criteria: Rf on thin-layer chromatography; incorporation of [1-14C]lignoceric acid and [3H]CoASH into the product; acid hydrolysis and identification of the radiolabel in lignoceric acid; and methanolysis and identification of the radiolabel in methyl lignocerate by thin-layer chromatography. The optimal concentrations for CoASH, ATP, and Mg2+ were about 100 microM, 10 mM, and 5 mM, respectively. Lignoceric acid, solubilized by alpha-cyclodextrin, Triton X-100, and deoxycholate, was utilized by the lignoceroyl-CoA ligase, but lignoceric acid solubilized by Triton WR-1339 was not. Topographical localization of lignoceroyl-CoA ligase in the plane of rat brain microsomal membranes was determined by the use of Triton X-100, trypsin, and mercury-Dextran, and was compared with the marker enzymes, ethanol acyltransferase and thiamine pyrophosphatase, which are known to be localized on the luminal (inner) surface of the microsomal vesicles. Mercury-Dextran (100 microM) and trypsin (trypsin:microsomes, 1:56 w/w) treatment of the microsomes inhibited the lignoceroyl-CoA ligase activity by 70 and 90% without disrupting the microsomal vesicles. Disruption of the vesicles with Triton X-100 increased the activity of both ethanol acyltransferase and thiamine pyrophosphatase by 400% but there was no increase in lignoceroyl-CoA ligase activity. These results suggest that lignoceroyl-CoA ligase is localized on the cytoplasmic surface of the microsomal vesicles.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclodextrins,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Dextrans,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Mercury,
http://linkedlifedata.com/resource/pubmed/chemical/Octoxynol,
http://linkedlifedata.com/resource/pubmed/chemical/Organomercury Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Thiamine Pyrophosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Cyclodextrins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-cyclodextrin,
http://linkedlifedata.com/resource/pubmed/chemical/mercury-dextran,
http://linkedlifedata.com/resource/pubmed/chemical/tyloxapol
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0003-9861
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
236
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
418-26
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:2578272-Adenosine Triphosphate,
pubmed-meshheading:2578272-Animals,
pubmed-meshheading:2578272-Brain,
pubmed-meshheading:2578272-Coenzyme A,
pubmed-meshheading:2578272-Coenzyme A Ligases,
pubmed-meshheading:2578272-Cyclodextrins,
pubmed-meshheading:2578272-Detergents,
pubmed-meshheading:2578272-Dextrans,
pubmed-meshheading:2578272-Female,
pubmed-meshheading:2578272-Magnesium,
pubmed-meshheading:2578272-Male,
pubmed-meshheading:2578272-Mercury,
pubmed-meshheading:2578272-Microsomes,
pubmed-meshheading:2578272-Octoxynol,
pubmed-meshheading:2578272-Organomercury Compounds,
pubmed-meshheading:2578272-Polyethylene Glycols,
pubmed-meshheading:2578272-Rats,
pubmed-meshheading:2578272-Rats, Inbred Strains,
pubmed-meshheading:2578272-Thiamine Pyrophosphatase,
pubmed-meshheading:2578272-Trypsin,
pubmed-meshheading:2578272-alpha-Cyclodextrins
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| pubmed:year |
1985
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| pubmed:articleTitle |
Lignoceroyl-CoA ligase activity in rat brain microsomal fraction: topographical localization and effect of detergents and alpha-cyclodextrin.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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