Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1982-12-21
|
pubmed:abstractText |
The pyruvate dehydrogenase and ATP-citrate(pro-3S)lyase activity in the liver after administration of nicotinic acid to chickens against a background of stimulated lypogenesis is shown to increase in the period of maximum fall of the acetyl-CoA-carboxylase activity. Affinity of ATP-citrate (pro-3S)-lyase to citrate at this time is lowered, the content of citrate and isocitrate is elevated and CoASac is decreased to some extent. A conclusion is made on the absence of substrate limitation of acetyl-CoA-carboxylase with administration of nicotinic acid to chickens under conditions of the fatty acid biosynthesis intensification.
|
pubmed:language |
rus
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0201-8470
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
54
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
530-4
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7135510-ATP Citrate (pro-S)-Lyase,
pubmed-meshheading:7135510-Animals,
pubmed-meshheading:7135510-Chickens,
pubmed-meshheading:7135510-Fatty Acids,
pubmed-meshheading:7135510-Kinetics,
pubmed-meshheading:7135510-Liver,
pubmed-meshheading:7135510-Niacin,
pubmed-meshheading:7135510-Pyruvate Dehydrogenase Complex
|
pubmed:articleTitle |
[Role of pyruvate dehydrogenase and ATP-citrate (pro-3S)lyase in inhibition of the biosynthesis of fatty acids by nicotinic acid].
|
pubmed:publicationType |
Journal Article,
English Abstract
|