Linked Life Data

6141763

Source:http://linkedlifedata.com/resource/pubmed/id/6141763

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-3-6
pubmed:abstractText
Two cAMP-independent acetyl-CoA carboxylase (ACC) protein kinases have been partially purified from rat liver cytosol and microsomal extracts. The first kinase, present in greatest activity in microsomal extracts, appears to be identical to casein kinase I by characteristic molecular size on gel filtration (Mr 40,000) and sodium dodecyl sulfate-gel electrophoresis (Mr 34,000), autophosphorylation of this single subunit, inability to efficiently utilize GTP, and resistance to inhibition by heparin and 2,3-diphosphoglycerate. The second kinase, predominant in cytosol, appears to be identical to casein kinase II by characteristic molecular size on gel filtration (Mr 150,000), an autophosphorylated subunit of Mr 25,000, a Km for GTP nearly equal to that of ATP, inhibition by heparin and 2,3 DPG, and relative substrate specificity. Despite the incorporation of up to 2 mol 32P/mol carboxylase subunit (kinase I) and 0.6 mol/subunit (kinase II), phosphorylation by either kinase causes no change in carboxylase activity. The site(s) phosphorylated by each kinase and by the cAMP-dependent protein kinase on carboxylase appear to be clustered on a Mr 16,000 cyanogen bromide peptide that is readily released on incubation with trypsin. The potential roles of these kinases in the regulation of ACC remain to be clarified.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
227
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
386-96
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Phosphorylation of acetyl-coenzyme A carboxylase by casein kinase I and casein kinase II.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.