Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-4-25
pubmed:abstractText
Dansyl-phosphatidylserine (D-PS) was used as a fluorescence probe to study interactions between protein kinase C (PKC) with phospholipid vesicles. It was found that D-PS fluorescence (520 nm) was enhanced by PKC (excited at 285 nm). The fluorescence energy transfer, indicative of a close association of PKC with D-PS vesicles, was differentially modulated by various phospholipids, depending upon their effects on PKC activation state and the manners in which they were present. PKC inhibitors (e.g. polymyxin B and ether lipids) potently inhibited the PKC-enhanced D-PS fluorescence. It is suggested that certain spatial arrangements between PKC and its phospholipid cofactor are essential for the enzyme activation and that D-PS would be a useful probe to study fluorimetrically such interactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
495-500
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Fluorimetric studies of protein kinase C interactions with phospholipids.
pubmed:affiliation
Department of Pharmacology, Emory University, Atlanta, Georgia 30322.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.