| pubmed-article:743253 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:743253 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:743253 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:743253 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:743253 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:743253 | lifeskim:mentions | umls-concept:C0391845 | lld:lifeskim |
| pubmed-article:743253 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:743253 | pubmed:dateCreated | 1979-4-25 | lld:pubmed |
| pubmed-article:743253 | pubmed:abstractText | 1. Lysosomes from rat liver contain two enzymic systems for hydrolysing phosphatidyl-inositol: a deacylation via lysophosphatidylinositol producing glycerophosphoinositol and non-esterified fatty acid, and a phospholipase C-like cleavage into inositol 1-phosphate and diaclygycerol. 2. The separate enzyme systems involved can be distinguished by gel filtration, differential temperature-stability and the inhibitory action of detergents. 3. The enzyme systems both have pH optima at 4.8 and their attack on a pure phosphatidylinositol substrate is inhibited by many bivalent metals including Ca2+ and Mg2+, and cationic drugs. 4. Whereas the deacylation system will attack other glycerophospholipids, the phospholipase C shows a marked specificity towards phosphatidylinositol, although it will also slowly attach phosphatidylcholine with the liberation of phosphocholine. 5. Gel filtration and temperature-stability distinguish the phospholipase C from lysosomal phosphatidic acid phosphatase, but not from sphingomyelinase. 6. Evidence is presented that an EDTA-insensitive phospholipase C degrading phosphatidylinositol is present in rat brain. | lld:pubmed |
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| pubmed-article:743253 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:743253 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:743253 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:743253 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:743253 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:743253 | pubmed:author | pubmed-author:DawsonR MRM | lld:pubmed |
| pubmed-article:743253 | pubmed:author | pubmed-author:IrvineR FRF | lld:pubmed |
| pubmed-article:743253 | pubmed:author | pubmed-author:HemingtonNN | lld:pubmed |
| pubmed-article:743253 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:743253 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:743253 | pubmed:volume | 176 | lld:pubmed |
| pubmed-article:743253 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:743253 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:743253 | pubmed:pagination | 475-84 | lld:pubmed |
| pubmed-article:743253 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:743253 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:743253 | pubmed:articleTitle | The hydrolysis of phosphatidylinositol by lysosomal enzymes of rat liver and brain. | lld:pubmed |
| pubmed-article:743253 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:743253 | pubmed:publicationType | In Vitro | lld:pubmed |
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