Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-2-5
pubmed:abstractText
Regulation of phosphatidylinositol 4-kinase (PtdIns 4-kinase) by protein tyrosine phosphorylation has been indirect and the effects of phosphorylation are debatable. Rat splenic type II PtdIns 4-kinase was phosphorylated in vitro with protein tyrosine kinases from Con A stimulated splenic lymphocytes. Stoichiometric analysis showed one mole of phosphate was incorporated per mole of PtdIns 4-kinase. Tyrosine phosphorylation increased the enzyme activity by 3-fold. Kinetic analysis showed a reduction in Km for PtdIns and an increase in Vmax. Dephosphorylation with protein phosphotyrosine phosphatase abolished the activation of PtdIns 4-kinase while protein phosphatase 2A had no effect. Protein tyrosine phosphorylation and activation of PtdIns 4-kinase appear to be tissue specific.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
441
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
432-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Protein tyrosine phosphorylation activates rat splenic type II phosphatidylinositol 4-kinase in vitro.
pubmed:affiliation
Biotechnology Centre, Indian Institute of Technology, Bombay Powai, Mumbai.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't