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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
42
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pubmed:dateCreated |
1993-11-26
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pubmed:abstractText |
Interphotoreceptor retinoid-binding protein (IRBP), a predominant protein in the interphotoreceptor matrix of the retina, has been implicated in transfer of retinoids between retinal pigment epithelium and photoreceptor cells. The interactions of IRBP with all-trans-retinol have been studied by three fluorescence-based methods and by measurements of binding of 3[H]-labeled all-trans-retinol to this protein. It was found that IRBP contains two sites with similar but not identical affinities for all-trans-retinol. The dissociation constant of the all-trans-retinol-IRBP complex at the first site was 0.1 microM, which is about 10-fold lower than previously reported values. The second site had about 2.5-fold lower affinity for all-trans-retinol as compared to the first site. Long-chain fatty acids were found in this study to displace all-trans-retinol from the stronger retinol-binding site on IRBP. Displacement of all-trans-retinol was used to study the interactions of fatty acids with this protein. It was found that docosahexaenoic acid (DHA C22:6n-3), an essential fatty acid which plays an important role in vision, had the highest apparent affinity for the site probed on IRBP of all the fatty acids studied.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Docosahexaenoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Nonesterified,
http://linkedlifedata.com/resource/pubmed/chemical/Retinol-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin A
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11311-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8218196-Animals,
pubmed-meshheading:8218196-Binding, Competitive,
pubmed-meshheading:8218196-Binding Sites,
pubmed-meshheading:8218196-Cattle,
pubmed-meshheading:8218196-Docosahexaenoic Acids,
pubmed-meshheading:8218196-Fatty Acids, Nonesterified,
pubmed-meshheading:8218196-Isomerism,
pubmed-meshheading:8218196-Kinetics,
pubmed-meshheading:8218196-Mathematics,
pubmed-meshheading:8218196-Photoreceptor Cells,
pubmed-meshheading:8218196-Retina,
pubmed-meshheading:8218196-Retinol-Binding Proteins,
pubmed-meshheading:8218196-Spectrometry, Fluorescence,
pubmed-meshheading:8218196-Tritium,
pubmed-meshheading:8218196-Vitamin A
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pubmed:year |
1993
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pubmed:articleTitle |
Interactions of all-trans-retinol and long-chain fatty acids with interphotoreceptor retinoid-binding protein.
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pubmed:affiliation |
Division of Nutritional Sciences, Cornell University, Ithaca, New York 14853.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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