Linked Life Data

169238

Source:http://linkedlifedata.com/resource/pubmed/id/169238

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1975-11-22
pubmed:abstractText
Heat-denatured chicken egg white lysozyme and the reduced carboxymethylated maleylated derivative of this protein were found to serve as substrates for rabbit skeletal muscle cyclic AMP-dependent protein kinase. The native form of the protein was not a substrate. Two phosphoryl groups per mole of lysozyme were incorporated in the reaction. It was determined that the phosphoryl moieties were bound to serine 24 and serine 50 in the modified protein. Serine 24 was phosphorylated approximately 3 times as fast as serine 50. Reduced carboxymethylated maleylated derivatives of bovine serum albumin, phosphorylase b, and creatine kinase also served as substrates for the protein kinase whereas their native forms did not. The reduced carboxymethylated maleylated derivative of the inhibitory subunit of troponin was a poorer substrate than the native form of the protein. Maleylated histones F1 and F2b were also poorer substrates than the nonderivatized forms. The significance of these experiments with reference to the specificity of cyclic AMP-dependent protein kinase is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6355-61
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Effect of denaturation on the susceptibility of proteins to enzymic phosphorylation.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.