| pubmed-article:8110188 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8110188 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8110188 | lifeskim:mentions | umls-concept:C0032043 | lld:lifeskim |
| pubmed-article:8110188 | lifeskim:mentions | umls-concept:C0054982 | lld:lifeskim |
| pubmed-article:8110188 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:8110188 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8110188 | pubmed:dateCreated | 1994-3-23 | lld:pubmed |
| pubmed-article:8110188 | pubmed:abstractText | Phosphatidylinositol synthase (CDP-1,2-diacyl-sn-glycerol:myoinositol 3-phosphatidyltransferase, EC 2.7.8.11) was purified from the microsomal fraction of human placenta. The Triton X-100-extracted enzyme was purified 8300-fold over the microsomal fraction by affinity chromatography on CDP-diacylglycerol-Sepharose followed by ion-exchange chromatography on Mono Q. The purified enzyme had a molecular mass of 24,000 Da on SDS/PAGE. The enzyme had a pH optimum at 9.0, required Mn2+ or Mg2+, and was inhibited by Ca2+ and Zn2+. The Km for myo-inositol was determined to be 0.28 mM. Optimal activity was obtained at 0.2-0.4 mM CDP-diacylglycerol; higher concentrations of the lipid substrate inhibited the enzyme reaction. The enzyme was inhibited by nucleoside di- and tri-phosphates, Pi and PPi. CDP competitively inhibited the enzyme reaction with a Kis of 4 mM. The optimal temperature for the PtdIns synthase reaction was 50 degrees C. | lld:pubmed |
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| pubmed-article:8110188 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8110188 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8110188 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8110188 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8110188 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8110188 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8110188 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8110188 | pubmed:author | pubmed-author:AntonssonB... | lld:pubmed |
| pubmed-article:8110188 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8110188 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8110188 | pubmed:volume | 297 ( Pt 3) | lld:pubmed |
| pubmed-article:8110188 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8110188 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8110188 | pubmed:pagination | 517-22 | lld:pubmed |
| pubmed-article:8110188 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8110188 | pubmed:meshHeading | pubmed-meshheading:8110188-... | lld:pubmed |
| pubmed-article:8110188 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8110188 | pubmed:articleTitle | Purification and characterization of phosphatidylinositol synthase from human placenta. | lld:pubmed |
| pubmed-article:8110188 | pubmed:affiliation | Glaxo Institute for Molecular Biology, Plan-les-Ouates/Geneva, Switzerland. | lld:pubmed |
| pubmed-article:8110188 | pubmed:publicationType | Journal Article | lld:pubmed |
| literatureCitation:3942_811... | literatureCitation:pubmed | pubmed-article:8110188 | lld:drugbank |
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