| pubmed-article:8049244 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8049244 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8049244 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:8049244 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8049244 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:8049244 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8049244 | lifeskim:mentions | umls-concept:C1529259 | lld:lifeskim |
| pubmed-article:8049244 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8049244 | pubmed:dateCreated | 1994-9-8 | lld:pubmed |
| pubmed-article:8049244 | pubmed:abstractText | The cDNA encoding mouse phosphatidylinositol transfer protein (PI-TP) was isolated by means of reverse transcriptase polymerase chain reaction. The nucleotide sequence of this cDNA has a high similarity (98%) with that of rat PI-TP; the predicted amino acid sequence is 99.6% identical to that of rat PI-TP. The cDNA encoding mouse PI-TP was cloned into the expression vector pET3d and the Escherichia coli strain BL21(DE3) was transformed with the resulting plasmid. After induction of the bacteria with isopropyl-beta-D-thiogalactopyranoside, PI-TP was efficiently expressed in the E. coli strain. It was estimated that 5% of the total soluble cell protein consisted of PI-TP. The recombinant mouse PI-TP was purified from the bacterial lysate in four steps: ammonium sulphate precipitation, anion-exchange chromatography, heparin-Sepharose affinity and gel filtration chromatography. Fractionation on the heparin-Sepharose affinity column yielded two forms: PI-TP Hepa1 and Hepa2. These two proteins have the same molecular mass of 35 kDa, both contain a phosphatidylglycerol molecule and both are recognized by anti-PI-TP antibody. Both recombinant proteins have an isoelectric point of 5.4 as compared to 5.5 for bovine brain PI-TP. Sequence analysis of the first 25 N-terminal amino acid residues showed that both forms are identical, except that PI-TP Hepa1 contains the initiator methionine which is lacking from PI-TP Hepa2. The two PI-TP forms have similar phospholipid-binding and transfer activity, comparable to that of bovine brain PI-TP. Both forms and bovine brain PI-TP are phosphorylated equally well in a Ca2+/phospholipid-dependent way by protein kinase C. | lld:pubmed |
| pubmed-article:8049244 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8049244 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8049244 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8049244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8049244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8049244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8049244 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8049244 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8049244 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:WirtzK WKW | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:WestermanJJ | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:BruningBB | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:SnoekG TGT | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:GeijtenbeekT... | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:de GrootEE | lld:pubmed |
| pubmed-article:8049244 | pubmed:author | pubmed-author:van BaalJJ | lld:pubmed |
| pubmed-article:8049244 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8049244 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:8049244 | pubmed:volume | 1213 | lld:pubmed |
| pubmed-article:8049244 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8049244 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8049244 | pubmed:pagination | 309-18 | lld:pubmed |
| pubmed-article:8049244 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:8049244 | pubmed:meshHeading | pubmed-meshheading:8049244-... | lld:pubmed |
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| pubmed-article:8049244 | pubmed:meshHeading | pubmed-meshheading:8049244-... | lld:pubmed |
| pubmed-article:8049244 | pubmed:meshHeading | pubmed-meshheading:8049244-... | lld:pubmed |
| pubmed-article:8049244 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8049244 | pubmed:articleTitle | Characterization of mouse phosphatidylinositol transfer protein expressed in Escherichia coli. | lld:pubmed |
| pubmed-article:8049244 | pubmed:affiliation | Centre for Biomembranes and Lipid Enzymology, University of Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:8049244 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8049244 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8049244 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:18738 | entrezgene:pubmed | pubmed-article:8049244 | lld:entrezgene |
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