| pubmed-article:6589591 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C0007125 | lld:lifeskim |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C0431085 | lld:lifeskim |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:6589591 | lifeskim:mentions | umls-concept:C0205296 | lld:lifeskim |
| pubmed-article:6589591 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:6589591 | pubmed:dateCreated | 1984-9-7 | lld:pubmed |
| pubmed-article:6589591 | pubmed:abstractText | A polypeptide-dependent protein kinase was purified about 80-fold from an extract of plasma membranes of Ehrlich ascites tumor cells. The membranes were extracted with Nonidet P-40, and the extract was purified by ammonium sulfate fractionation and hydroxylapatite and affinity chromatography. The activity was stimulated 10-fold or more by polypeptide preparations from a variety of tissues, including placenta and hypothalamus. Polypeptide-dependent protein kinase had a pH optimum of about 7.5 and required Mg2+ for activity. Mn2+ at low concentrations (200 microM) stimulated enzyme activity somewhat but inhibited activity strongly at higher concentrations. The best available substrate for polypeptide-dependent protein kinase was beta-casein, and little or no phosphorylation was observed with alpha-casein, kappa-casein, phosvitin, alpha-lactalbumin, alpha-lactoglobulin, and histone. However, several endogenous substrates from plasma membranes of Ehrlich ascites tumor cells were phosphorylated. Polypeptide-dependent protein kinase activity was not inhibited by 10 mM N-ethylmaleimide, and this resistance was useful in differentiating this protein kinase from other protein kinases that were present in crude fractions and sensitive to the inhibitor. | lld:pubmed |
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| pubmed-article:6589591 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6589591 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6589591 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6589591 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:6589591 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:6589591 | pubmed:author | pubmed-author:RackerEE | lld:pubmed |
| pubmed-article:6589591 | pubmed:author | pubmed-author:Abdel-GhanyMM | lld:pubmed |
| pubmed-article:6589591 | pubmed:author | pubmed-author:BlairE AEA | lld:pubmed |
| pubmed-article:6589591 | pubmed:author | pubmed-author:SherrillKK | lld:pubmed |
| pubmed-article:6589591 | pubmed:author | pubmed-author:RieglerCC | lld:pubmed |
| pubmed-article:6589591 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6589591 | pubmed:volume | 81 | lld:pubmed |
| pubmed-article:6589591 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6589591 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6589591 | pubmed:pagination | 4250-4 | lld:pubmed |
| pubmed-article:6589591 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:6589591 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6589591 | pubmed:articleTitle | New protein kinase from plasma membrane of Ehrlich ascites tumor cells activated by natural polypeptides. | lld:pubmed |
| pubmed-article:6589591 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6589591 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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