Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-10
pubmed:abstractText
The binding of protein kinase C (PKC) to pyrene-labeled diacylglycerol (pDG) has been studied in a mixed micellar system by monitoring resonance energy transfer from excited tryptophans to pyrene with time-correlated single photon counting. The average lifetime of the excited state of the tryptophans in PKC showed a clear dependence on the mole percentage pDG in micelles in contrast with pyrene-labeled phosphatidylcholine (pPC). The binding data has been analyzed to a simple model which encompasses the size of the micelles and the binding constant of the pDG-PKC complex. From our data, though, these quantities cannot be determined independently. If we have no size information on the micelles we can determine a lower boundary of this quantity compatible with the data. When the micellar size is known, a binding constant for the DG-PKC complex can be extracted. The presented analytical approach can be applied to other systems in which lipid-protein interactions must be quantified.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-91
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The interaction of pyrene labeled diacylglycerol with protein kinase C in mixed micelles.
pubmed:affiliation
Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't