Linked Life Data

3355559

Source:http://linkedlifedata.com/resource/pubmed/id/3355559

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-5-11
pubmed:abstractText
Ca2+/CaM-dependent multifunctional protein kinase isoenzymes from brain, skeletal muscle and liver were compared by their phosphorylation of a number of protein substrates. Under the conditions of assay, the three isoenzymes demonstrated rapid phosphorylation of synapsin I and glycogen synthase. In contrast, rates of phosphorylation of pyruvate kinase and phenylalanine hydroxylase were almost two orders of magnitude slower. Differences in phosphorylation specifically of the latter two substrates was also observed among the three protein kinases. Phosphorylation by Ca2+/CaM-dependent protein kinases was contrasted with cAMP-dependent protein kinase, which phosphorylates these proteins in vitro and in vivo. The potential role of Ca2+/CaM-dependent multifunctional protein kinases in the Ca2+-dependent phosphorylation of these substrates is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1332-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Substrate specificity of Ca2+/CaM-dependent multifunctional protein kinases: comparison of isoenzymes from brain, liver and skeletal muscle.
pubmed:affiliation
University of Texas Medical School, Department of Pharmacology, Houston 77025.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.