Linked Life Data

9705216

Source:http://linkedlifedata.com/resource/pubmed/id/9705216

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-9-16
pubmed:abstractText
The peptides N-biotinyl-RRRCLRRL and N-biotinyl-RKRCLRRL covalently modify protein kinase C (PKC) through reaction of the Cys sulfhydryl group with the active site of the enzyme. The labeling of PKC occurs only in the presence of the cofactors phosphatidylserine, diacylglycerol, and Ca2+ but not in their absence. Low concentrations of the Arg-rich substrate, R4YGSR6Y greatly increase the extent of the reaction of these biotinylated peptides with PKC in the presence of lipid cofactors but in the absence of calcium. This effect can be observed at 50 nM R4YGSR6Y and suggests the presence of a high-affinity binding site for Arg-rich peptides which is separate from the active site but which enhances accessibility of the active site. The study also demonstrates the utility of the biotinylated peptides as active site labels which can detect the conformational change accompanying the activation of PKC.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0003-9861
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
356
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
258-64
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Evidence for a regulatory binding site for arginine-rich peptides on protein kinase C.
pubmed:affiliation
Department of Biochemistry, McMaster University, 1200 Main Street West, Hamilton, Ontario, L8N 3Z5, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't