Linked Life Data

33166

Source:http://linkedlifedata.com/resource/pubmed/id/33166

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-4-25
pubmed:abstractText
A hormonally induced change in the covalent phosphorylation state of several enzymes is generally regarded as an important mechanism for hormonal modulation of enzyme activity. We have previously demonstrated that epinephrine stimulates the phosphorylation of a peptide of Mr = 220,000 in adipocytes. Incubation of 32P-labeled cytosolic proteins from adipocytes and hepatocytes with antisera raised against homogeneous chicken and rat liver acetyl coenzyme A carboxylase results in the specific and complete precipitation of the same phosphopeptide. No other major phosphopeptide is specifically precipitated. In hepatocytes, glucagon stimulates the incorporation of 32P into this peptide associated with an inhibition of enzyme activity. These data, coupled with previous studies in adipocytes, suggest that cyclic AMP-dependent protein phosphorylation plays a major role in the regulation of acetyl-CoA carboxylase activity and of fatty acid biosynthesis in adipose tissue and liver.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Glucagon regulation of protein phosphorylation. Identification of acetyl coenzyme A carboxylase as a substrate.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.