| pubmed-article:681278 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:681278 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:681278 | lifeskim:mentions | umls-concept:C0085491 | lld:lifeskim |
| pubmed-article:681278 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:681278 | lifeskim:mentions | umls-concept:C1550101 | lld:lifeskim |
| pubmed-article:681278 | lifeskim:mentions | umls-concept:C0150312 | lld:lifeskim |
| pubmed-article:681278 | lifeskim:mentions | umls-concept:C0061576 | lld:lifeskim |
| pubmed-article:681278 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:681278 | pubmed:dateCreated | 1978-10-25 | lld:pubmed |
| pubmed-article:681278 | pubmed:abstractText | Human erythrocyte membrane glycerophospholipids are deacylated by Aeromonas hydrophila 13-h culture supernatants, resulting in the production of cholesterol ester, free fatty acid, and water-soluble phosphates. This activity appears to be due to the actions of an acyltransferase (phosphatide:cholesterol acyltransferase, EC 2.3.1 group) and a phospholipase (phosphatide acyl-hydrolase). The enzyme activities are produced simultaneously in late exponential/early stationary phase, are precipitated together from the culture supernatant with 85% ammonium sulfate, and are eluted together near the void volume during gel filtration on Sepharose 6B. These results suggest that A. hydrophila produces a multienzyme complex with an unusual mode of action on membrane lipids. The complex is distinct from the hemolytic factor aerolysin, which is also produced by A. hydrophila. | lld:pubmed |
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| pubmed-article:681278 | pubmed:language | eng | lld:pubmed |
| pubmed-article:681278 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:681278 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:681278 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:681278 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:681278 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:681278 | pubmed:author | pubmed-author:BuckleyJ TJT | lld:pubmed |
| pubmed-article:681278 | pubmed:author | pubmed-author:MacIntyreSS | lld:pubmed |
| pubmed-article:681278 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:681278 | pubmed:volume | 135 | lld:pubmed |
| pubmed-article:681278 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:681278 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:681278 | pubmed:pagination | 402-7 | lld:pubmed |
| pubmed-article:681278 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:681278 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:681278 | pubmed:articleTitle | Presence of glycerophospholipid: cholesterol acyltransferase and phospholipase in culture supernatant of Aeromonas hydrophila. | lld:pubmed |
| pubmed-article:681278 | pubmed:publicationType | Journal Article | lld:pubmed |
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