Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-3-23
pubmed:abstractText
Insulin-stimulated protein kinase activities detected in Xenopus oocyte membrane were examined. The plasma membrane proteins solubilized in a buffer containing Triton X-100 were immunoprecipitated with anti-phosphotyrosine antibodies and adsorbed materials were eluted with a buffer containing p-nitrophenyl phosphate. The eluate contained protein serine kinase activity toward H1 histone which was increased 2-3 fold by insulin. Protein tyrosine kinase activity was also exhibited in Xenopus oocyte membrane and the close parallel to serine kinase activity was observed in response to insulin. These results suggest that insulin-stimulated serine kinase is activated through the phosphorylation by protein tyrosine kinase.
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
15
pubmed:volume
150
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1176-84
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Insulin-stimulated serine kinase in Xenopus oocyte plasma membrane.
pubmed:affiliation
Department of Biochemistry, Fukui Medical School, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't