Linked Life Data

1847631

Source:http://linkedlifedata.com/resource/pubmed/id/1847631

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-3-27
pubmed:abstractText
Phosphofructokinase (PFK) from sheep heart was shown to be phosphorylated by Ca2+/calmodulin protein kinase (CaM-kinase) as well as by cyclic AMP-dependent protein kinase (PKA). HPLC analysis of phosphorylated PFK indicated that phosphorylation by CaM-kinase occurs at least at two sites that are distinct from those recognized by PKA. Phosphorylation by either CaM-kinase of PKA resulted in an increase in sensitivity to ATP inhibition and a small but consistent decrease in Ki for ATP. Phosphorylation by either protein kinase caused a slight increase in the Km of PFK for fructose-6-P. Protein kinase C failed to phosphorylate PFK. Combinations of PKA, CaM-kinase and protein kinase C did not alter the stoichiometry of phosphorylation and did not change the effect on enzyme activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
174
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1255-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Phosphorylation of heart phosphofructokinase by Ca2+/calmodulin protein kinase.
pubmed:affiliation
Department of Pharmacology, Stanford University School of Medicine, California 94305.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.