Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1980-11-24
pubmed:abstractText
2-Stearoyl spin-labeled phosphatidylcholine (PC*) has been introduced into the phosphatidylcholine exchange protein from bovine liver and its electron spin resonance (ESR) spectrum determined. The spin-labeled group in the PC*- exchange protein complex was strongly immobilized. Addition of sodium deoxycholate micelles released PC* from its binding site, producing a mobile signal. This was also observed when micelles of lysophosphatidylcholine and vesicles of phosphatidic acid were added, indicating that the exchange protein can insert its endogenous PC* into interfaces devoid of phosphatidylcholine. ESR spectroscopy was used to measure transfer of PC* from spin-labeled "donor" vesicles to unlabeled "acceptor" vesicles as described by Machida & Ohnishi [Machida, K., & Ohnishi, S. (1978) Biochim. Biophys. Acta 507, 156-164]. The donor vesicles consisted of PC* and phosphatidic acid (75:25 mol%) and the acceptor vesicles of phosphatidylethanolamine and phosphatidic acid (81:19 mol%). Addition of exchange protein catalyzed a net transfer of PC* from donor to acceptor vesicles. This transfer proceeded until the acceptor vesicles contained approximately 2 mol% of PC*. A spontaneous transfer of PC* was not observed. As for the mode of action, it appears that the exchange protein, after insertion of its endogenous PC* into the acceptor, leaves the interface without a bound phospholipid molecule yet continues to shuttle PC* from donor to acceptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3395-9
pubmed:dateRevised
2006-11-20
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Phosphatidylcholine exchange protein catalyzes the net transfer of phosphatidylcholine to model membranes.
pubmed:publicationType
Journal Article