| pubmed-article:2539091 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2539091 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:2539091 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:2539091 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:2539091 | lifeskim:mentions | umls-concept:C0054982 | lld:lifeskim |
| pubmed-article:2539091 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2539091 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2539091 | pubmed:dateCreated | 1989-4-25 | lld:pubmed |
| pubmed-article:2539091 | pubmed:abstractText | Solubilization of phosphatidylinositol (PtdIns) synthase (CDP-diacylglycerol: myo-inositol 3-phosphatidyltransferase, EC 2.7.8.11) from rat pituitary (GH3) tumours was investigated. PtdIns synthase activity was partially extracted from crude membranes by 3 M-KCl. Prior separation of membranes revealed that a greater proportion of plasma-membrane PtdIns synthase activity was salt-extractable than was endoplasmic reticulum activity. The activity of the salt-extracted enzyme was maximized by low concentrations of 3-(3-cholamidopropyl) dimethylammonio-1-propanesulphonate (CHAPS; 0.5 mM), Triton X-100 (0.1 mM) or a phospholipid mixture (0.05 mg/ml), but higher concentrations of detergents were inhibitory. The activity of salt-extracted PtdIns synthase was 0.25 +/- 0.08 nmol/min per mg of protein. Salt-extracted PtdIns synthase activity was dependent on Mg2+ (maximal at 0.1 mM) and Mn2+ (maximal at 5 mM), and its pH optimum was in the range 7.0-7.5. The apparent Km for myo-inositol (in the presence of 0.1 mM-CDP-diacylglycerol) was 0.06 mM, and that for CDP-diacylglycerol (at 0.1 mM-myo-inositol) was 0.21 mM. Salt-extracted PtdIns synthase activity was potently inhibited by Ca2+ (50% inhibition at 1 microM), with over 90% inhibition at 10 microM-Ca2+. These data imply the existence of two forms of membrane-associated PtdIns synthase, namely salt-extractable and salt-resistant, with different intracellular localizations. The salt-extractable form of this enzyme may be a useful preparation for further characterization and purification of mammalian PtdIns synthase. | lld:pubmed |
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| pubmed-article:2539091 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2539091 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2539091 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2539091 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2539091 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2539091 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2539091 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2539091 | pubmed:author | pubmed-author:GershengornM... | lld:pubmed |
| pubmed-article:2539091 | pubmed:author | pubmed-author:CubittA BAB | lld:pubmed |
| pubmed-article:2539091 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2539091 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2539091 | pubmed:volume | 257 | lld:pubmed |
| pubmed-article:2539091 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2539091 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2539091 | pubmed:pagination | 639-44 | lld:pubmed |
| pubmed-article:2539091 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2539091 | pubmed:meshHeading | pubmed-meshheading:2539091-... | lld:pubmed |
| pubmed-article:2539091 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2539091 | pubmed:articleTitle | Characterization of a salt-extractable phosphatidylinositol synthase from rat pituitary-tumour membranes. | lld:pubmed |
| pubmed-article:2539091 | pubmed:affiliation | Department of Medicine, Cornell University Medical College, New York, NY. | lld:pubmed |
| pubmed-article:2539091 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2539091 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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