| pubmed-article:2543374 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C0004597 | lld:lifeskim |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C0089795 | lld:lifeskim |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
| pubmed-article:2543374 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
| pubmed-article:2543374 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2543374 | pubmed:dateCreated | 1989-7-3 | lld:pubmed |
| pubmed-article:2543374 | pubmed:abstractText | Phosphatidylinositol-specific phospholipase C (PI-PLC) produced by Bacillus thuringiensis has been used as a probe for the distribution of phosphatidylinositol in hepatocyte membranes. Approx. 50% of this phospholipid was hydrolysed in microsomal vesicles (endoplasmic reticulum) with no significant hydrolysis of the remaining membrane phospholipids. Latency of mannose-6-phosphatase was retained during treatment indicating that the vesicles remained impermeable. Stripping of the ribosomes did not increase hydrolysis of phosphatidylinositol; however, when the vesicles were opened using dilute sodium carbonate, hydrolysis increased to greater than 90%. Hydrolysis of phosphatidylinositol of Golgi membranes was 35% and of plasma membranes was 50%. After treatment with PI-PLC, radiolabelled secretory proteins were retained in Golgi membranes and trapped lactate dehydrogenase was retained in plasma-membrane preparations indicating that the vesicles remained closed. Hydrolysis of phosphatidylinositol increased to greater than 90% when the membranes were opened by treatment with dilute sodium carbonate. These observations indicate that PI-PLC of Bacillus thuringiensis is a suitable probe for the distribution of phosphatidylinositol in membranes, and that in liver membranes this phospholipid occurs on each side of the bilayer, a topography consistent with its diverse roles. | lld:pubmed |
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| pubmed-article:2543374 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2543374 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2543374 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2543374 | pubmed:month | May | lld:pubmed |
| pubmed-article:2543374 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2543374 | pubmed:author | pubmed-author:HigginsJ AJA | lld:pubmed |
| pubmed-article:2543374 | pubmed:author | pubmed-author:OjaS SSS | lld:pubmed |
| pubmed-article:2543374 | pubmed:author | pubmed-author:HitchinB WBW | lld:pubmed |
| pubmed-article:2543374 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2543374 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2543374 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:2543374 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2543374 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2543374 | pubmed:pagination | 913-6 | lld:pubmed |
| pubmed-article:2543374 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2543374 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2543374 | pubmed:articleTitle | Phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis as a probe for the distribution of phosphatidylinositol in hepatocyte membranes. | lld:pubmed |
| pubmed-article:2543374 | pubmed:affiliation | Department of Molecular Biology and Biotechnology, University of Sheffield, U.K. | lld:pubmed |
| pubmed-article:2543374 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2543374 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2543374 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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