Linked Life Data

2790054

Source:http://linkedlifedata.com/resource/pubmed/id/2790054

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-10-28
pubmed:abstractText
The incorporation of tritiated retinoic acid into proteins has been studied in cell-free extracts from rat liver and kidney. Incubation with retinoic acid in the presence of ATP and CoA resulted in a CoA intermediate. This CoA intermediate is a substrate for enzymes that incorporate the labeled retinoic acid moiety into proteins (Mr = 14,000-60,000) as detected with SDS-polyacrylamide gel electrophoresis. In the microsomal fraction, the label was found in a single protein (Mr 30,000). Retinoic acid is linked to the protein via a thioester bond as indicated by neutral hydrolysis with hydroxylamine and the bond's sensitivity to reducing agent. The incorporation of labeled retinoic acid into the protein is very rapid but decreases upon prolonged incubation, suggesting a high turnover of retinoic acid in the protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
998
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Incorporation of retinoic acid into proteins via retinoyl-CoA.
pubmed:affiliation
Department of Biochemistry, University of Wisconsin-Madison, College of Agricultural and Life Sciences, Madison.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't