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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1992-9-14
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pubmed:abstractText |
Retinol decomposes rapidly into a number of products, including its aldehyde form, retinal, when introduced into buffer in phospholipid vesicles or ethanol. Interphotoreceptor retinoid-binding protein at low concentrations is found to protect retinol from isomerization and oxidation. The addition of alpha-tocopherol to either liposomes or an ethanolic-buffer solution also prevents decomposition. Neither of these agents interferes with the successful regeneration of pigment with 9-cis retinal in rod outer segment preparations or the restoration of sensitivity by retinoids in isolated rod photoreceptors.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0031-8655
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1502268-Animals,
pubmed-meshheading:1502268-Cattle,
pubmed-meshheading:1502268-Isomerism,
pubmed-meshheading:1502268-Oxidation-Reduction,
pubmed-meshheading:1502268-Photochemistry,
pubmed-meshheading:1502268-Retinol-Binding Proteins,
pubmed-meshheading:1502268-Rod Cell Outer Segment,
pubmed-meshheading:1502268-Vitamin A,
pubmed-meshheading:1502268-Vitamin E
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pubmed:year |
1992
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pubmed:articleTitle |
Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol.
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pubmed:affiliation |
Department of Ophthalmology, Medical University of South Carolina, Charleston 29425.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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