Linked Life Data

1959595

Source:http://linkedlifedata.com/resource/pubmed/id/1959595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1992-1-7
pubmed:abstractText
The relationship and substrate specificity of the human erythrocyte membrane kinase and casein kinase A were investigated. Based on Staphylococcus aureus V8 protease digestion patterns, the 2 kinases appeared to be structurally homologous. These enzymes also exhibited the same substrate specificity and phosphorylated the same synthetic peptides and domains of ankyrin. Both kinases did not utilize GTP effectively as a substrate and were not inhibited by low concentrations of heparin, suggesting that they were type I casein kinases. An analysis of synthetic peptide phosphorylation failed to reveal a specific pattern of recognition of the amino acid sequence surrounding the phosphorylation site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
292
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Identity and substrate specificity of human erythrocyte membrane-bound and cytosolic casein kinases.
pubmed:affiliation
Department of Biochemistry, University of Illinois, Chicago 60612.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.