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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
28
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pubmed:dateCreated |
1996-8-29
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pubmed:databankReference |
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pubmed:abstractText |
Isolation and characterization of a rat brain cDNA identified a third acyl-CoA synthetase (ACS) designated ACS3. The deduced amino acid sequence of the cDNA revealed that ACS3 consists of 720 amino acids and exhibits a structural architecture common to ACSs from various origins. ACS3 expressed in COS cells was purified to near homogeneity. The purified ACS3 resolved by SDS-polyacrylamide gel electrophoresis into two major proteins of 79 and 80 kDa. Cell-free translation of a synthetic mRNA encoding the entire region of ACS3 revealed that the two isoforms were derived from the same mRNA. The purified ACS3 utilizes laurate and myristate most efficiently among C8-C22 saturated fatty acids and arachidonate and eicosapentaenoate among C16-C20 unsaturated fatty acids. Northern blot analysis revealed that ACS3 mRNA is most abundant in brain and, to a much lesser extent, in lung, adrenal gland, kidney, and small intestine. During the development of the rat brain, expression of ACS3 mRNA reached a maximum level at 15 days after birth and then declined gradually to 10% of the maximum in the adult brain.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/FAA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/long-chain-fatty-acid-CoA ligase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16748-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8663269-Amino Acid Sequence,
pubmed-meshheading:8663269-Animals,
pubmed-meshheading:8663269-Base Sequence,
pubmed-meshheading:8663269-Brain,
pubmed-meshheading:8663269-Cell Line,
pubmed-meshheading:8663269-Coenzyme A Ligases,
pubmed-meshheading:8663269-DNA, Complementary,
pubmed-meshheading:8663269-Fatty Acids,
pubmed-meshheading:8663269-Gene Expression Regulation, Developmental,
pubmed-meshheading:8663269-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8663269-Isoenzymes,
pubmed-meshheading:8663269-Kinetics,
pubmed-meshheading:8663269-Molecular Sequence Data,
pubmed-meshheading:8663269-RNA, Messenger,
pubmed-meshheading:8663269-Rats,
pubmed-meshheading:8663269-Repressor Proteins,
pubmed-meshheading:8663269-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8663269-Substrate Specificity
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pubmed:year |
1996
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pubmed:articleTitle |
Molecular characterization and expression of rat acyl-CoA synthetase 3.
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pubmed:affiliation |
Tohoku University Gene Research Center, 1-1 Tsutsumidori-Amamiya, Aoba, Sendai 981, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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