| pubmed-article:6095827 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C0039005 | lld:lifeskim |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C0018183 | lld:lifeskim |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:6095827 | lifeskim:mentions | umls-concept:C1521827 | lld:lifeskim |
| pubmed-article:6095827 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6095827 | pubmed:dateCreated | 1985-1-2 | lld:pubmed |
| pubmed-article:6095827 | pubmed:abstractText | Plasma membranes prepared from pig granulocytes were incubated in the presence of [gamma-32P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated the incorporation of 32P into both the protein and lipid fractions of the membrane. The SDS gel-electrophoretic analysis of the 32P-labelled proteins showed that the protein kinase phosphorylated preferentially a 24000-Mr protein, though other 32P-labelled proteins were also detected. 32P-labelled membrane lipids were analysed in two different thin layer chromatographic systems. 32P-labelling was found exclusively in polyphosphoinositides. On addition of the protein kinase the 32P-labelling of both polyphosphoinositides was increased but a higher amount of phosphate was incorporated into phosphatidylinositol-4-phosphate than into phosphatidylinositol-4,5-bisphosphate. | lld:pubmed |
| pubmed-article:6095827 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6095827 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6095827 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6095827 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6095827 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6095827 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:6095827 | pubmed:author | pubmed-author:GárdosGG | lld:pubmed |
| pubmed-article:6095827 | pubmed:author | pubmed-author:SarkadiBB | lld:pubmed |
| pubmed-article:6095827 | pubmed:author | pubmed-author:NagyZZ | lld:pubmed |
| pubmed-article:6095827 | pubmed:author | pubmed-author:FaragóAA | lld:pubmed |
| pubmed-article:6095827 | pubmed:author | pubmed-author:FarkasGG | lld:pubmed |
| pubmed-article:6095827 | pubmed:author | pubmed-author:EnyediAA | lld:pubmed |
| pubmed-article:6095827 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6095827 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:6095827 | pubmed:volume | 124 | lld:pubmed |
| pubmed-article:6095827 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6095827 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6095827 | pubmed:pagination | 871-6 | lld:pubmed |
| pubmed-article:6095827 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:meshHeading | pubmed-meshheading:6095827-... | lld:pubmed |
| pubmed-article:6095827 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6095827 | pubmed:articleTitle | Cyclic AMP-dependent protein kinase stimulates the phosphorylation of phosphatidylinositol to phosphatidylinositol-4-monophosphate in a plasma membrane preparation from pig granulocytes. | lld:pubmed |
| pubmed-article:6095827 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6095827 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6095827 | lld:pubmed |
