Linked Life Data

1998517

Source:http://linkedlifedata.com/resource/pubmed/id/1998517

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-4-3
pubmed:abstractText
Rat liver cytosolic fraction caused up to five fold stimulation of mitochondrial glycerophosphate acyltransferase apparently by removing the lysophosphatidic acid formed by the acyltransferase. When mitochondria were incubated with palmityl-CoA, [2-3H]-sn-glycerol 3-phosphate and the cytosolic fraction and the supernatant fluid of the incubated mixture was passed through a Sephadex G-100 column, labeled lysophosphatidic acid eluted in three peaks with Mrs (i) 60-70 kDa, (ii) 10-20 kDa, and (iii) less than 5 kDa. Proteins, responsible for binding of lysophosphatidic acid in peaks (i) and (ii), were purified to near homogeneity as judged by electrophoretic analysis. The lysophosphatidic acid binding protein in peak (i) appears to be serum albumin and peak (iii) represents largely unbound lysophosphatidic acid. The 15 kDa protein, purified from peak (ii), bound lysophosphatidic acid, stimulated the acyltransferase and export of lysophosphatidic acid from mitochondria.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
175
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
339-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
A lysophosphatidic acid-binding cytosolic protein stimulates mitochondrial glycerophosphate acyltransferase.
pubmed:affiliation
Department of Biological Sciences, St. John's University, Jamaica, New York 11439.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.