Linked Life Data

6113263

Source:http://linkedlifedata.com/resource/pubmed/id/6113263

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-8-10
pubmed:abstractText
Rat liver acetyl-CoA carboxylase has been purified to homogeneity by a new method involving polyethylene glycol precipitation, and DEAE and Sepharose 4B chromatography. The final product displays a single band on SDS polyacrylamide gel electrophoresis of estimated molecular weight 240,000. This material contains 5.5 +/- 0.3 moles of alkali-labile phosphate per subunit and has a specific activity of 1.2 +/- 0.2 units per mg protein. As compared to previous purification procedures for the liver enzyme, this product has a higher phosphate content, lower specific activity, and an absence of major proteolysis. Trypsin digestion of 32P-labeled acetyl-CoA carboxylase from hepatocytes reveals that the 32P-labeled phosphorylation sites are extremely labile to proteolytic digestion. Potential modification of isolated liver acetyl-CoA carboxylase by proteolysis and/or dephosphorylation must be ascertained prior to in vitro enzymatic studies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2275
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
364-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
A new method for the isolation of rat liver acetyl-CoA carboxylase.
pubmed:publicationType
Journal Article