Linked Life Data

218622

Source:http://linkedlifedata.com/resource/pubmed/id/218622

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1979-6-29
pubmed:abstractText
Reaction of the cAMP (cyclic adenosine 3'--5'-monophosphate) receptor protein (CRP) of Escherichia coli with the bifunctional reagent o-phenylenedimaleimide (oPDM) results in the cross-linking of the two subunits of a CRP protomer. In the presence of cAMP the rate of cross-linking increases. CRP modified with oPDM retains [3H]cAMP binding activity but loses [3H]d(I-C)n binding activity. Proteolysis of cross-linked CRP gives distinct sodium dodecyl sulfate-polyacrylamide gel electrophoretic patterns depending upon whether cAMP was present during the reaction with oPDM. CRP cross-linked in the absence of cAMP retains the same relative resistance to proteolysis as unmodified CRP. The presence of 0.1 mM cAMP during proteolysis results in the production of two fragments, one of approximately 13 000 daltons and a second of approximately 20 000 daltons. CRP cross-linked with oPDM in the presence of cAMP (then dialyzed to remove cAMP) remains sensitive to alpha-chymotrypsin digestion even in the absence of added cAMP producing only the 13 000-dalton fragment. It is suggested that the nature of the oPDM cross-link is a consequence of the conformational state of CRP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1519-25
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Cross-linking of the cAMP receptor protein of Escherichia coli by o-phenylenedimaleimide as a probe of conformation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.