Linked Life Data

3178828

Source:http://linkedlifedata.com/resource/pubmed/id/3178828

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-11-21
pubmed:abstractText
This report demonstrates that exogenous phosphatidylcholine will serve as an acyl donor for the esterification of retinol complexed to cellular retinol-binding protein (CRBP) by human and rat liver microsomal preparations. The retinyl ester synthases utilized phosphatidylcholine but had little or no ability to transfer acyl groups from lysophosphatidylcholine, phosphatidyl-ethanolamine, or phosphatidic acid to retinol-CRBP. The human and rat activities also demonstrated positional selectivity as only the fatty acyl group at the sn-1 position of phosphatidylcholine was transferred. This in vitro activity may have considerable physiological importance since the fatty acyl composition at the sn-1 position of phosphatidylcholine is remarkably similar to the hepatic retinyl esters observed in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
156
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
A lecithin:retinol acyltransferase activity in human and rat liver.
pubmed:affiliation
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
pubmed:publicationType
Journal Article