| pubmed-article:8457568 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8457568 | lifeskim:mentions | umls-concept:C1416905 | lld:lifeskim |
| pubmed-article:8457568 | lifeskim:mentions | umls-concept:C0178463 | lld:lifeskim |
| pubmed-article:8457568 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8457568 | pubmed:dateCreated | 1993-4-27 | lld:pubmed |
| pubmed-article:8457568 | pubmed:abstractText | Lecithin retinol acyltransferase (LRAT) transfers acyl groups regiospecifically from the sn-1 position of lecithins to all-trans-retinol (vitamin A) and similar retinoids. LRAT is essential for the biosynthesis of 11-cis-retinal, the visual pigment chromophore. LRAT is also required for the general dietary mobilization of vitamin A. The enzyme is membrane-bound and has been solubilized and partially, but not completely, purified. It is demonstrated here that all-trans-retinyl alpha-bromoacetate (RBA) is a potent irreversible affinity labeling agent of LRAT. The measured KI = 12.1 microM and the pseudo-first-order rate constant for inhibition is kinh = 8.2 x 10(-4) s-1. The specificity of the inhibition process is further evidenced by the observation that alpha-bromoacetate derivatives of hydrophobic alcohols which are not substrates for LRAT, such as cholesterol and beta-ionol, are not inhibitors of the enzyme. Labeling of the partially purified enzyme with 3H-RBA showed a single radiolabeled band of molecular weight approximately 25,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. | lld:pubmed |
| pubmed-article:8457568 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8457568 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8457568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8457568 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8457568 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8457568 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8457568 | pubmed:author | pubmed-author:RandoR RRR | lld:pubmed |
| pubmed-article:8457568 | pubmed:author | pubmed-author:NyoM MMM | lld:pubmed |
| pubmed-article:8457568 | pubmed:author | pubmed-author:FuruyoshiSS | lld:pubmed |
| pubmed-article:8457568 | pubmed:author | pubmed-author:HubacekII | lld:pubmed |
| pubmed-article:8457568 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8457568 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:8457568 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8457568 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8457568 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8457568 | pubmed:pagination | 3077-80 | lld:pubmed |
| pubmed-article:8457568 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
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| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
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| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
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| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
| pubmed-article:8457568 | pubmed:meshHeading | pubmed-meshheading:8457568-... | lld:pubmed |
| pubmed-article:8457568 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8457568 | pubmed:articleTitle | Affinity labeling of lecithin retinol acyltransferase. | lld:pubmed |
| pubmed-article:8457568 | pubmed:affiliation | Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115. | lld:pubmed |
| pubmed-article:8457568 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8457568 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8457568 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8457568 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8457568 | lld:pubmed |
