Linked Life Data

2829478

Source:http://linkedlifedata.com/resource/pubmed/id/2829478

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-3-14
pubmed:abstractText
Plasma membrane preparation obtained from isolated mouse hepatocytes was phosphorylated by exogenous cyclic AMP dependent protein kinase in the presence of 32P-ATP. The phosphorylated proteins were analysed by SDS-polyacrylamide gel-electrophoresis of the membrane and the phosphorylated lipids were analysed by thin layer chromatography of the separated lipid fraction. The protein kinase stimulated the 32P incorporation into phosphatidylinositol 4-phosphate and it catalyzed the phosphorylation of several proteins. The main phosphoprotein bands were found at 51 kDa, 49 kDa, 46 kDa and 34 kDa. A part of the 51 kDa phosphoprotein accompanied the lipids in the course of the separation of the lipid fraction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0237-6261
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-16
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The effect of the cAMP-dependent protein kinase on protein phosphorylation and phosphatidylinositol 4-phosphate formation in a hepatocyte membrane preparation.
pubmed:affiliation
1st Institute of Biochemistry, Semmelweis University Medical School, Budapest, Hungary.
pubmed:publicationType
Journal Article, In Vitro