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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-7-16
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pubmed:abstractText |
Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic acid receptors, a number of structurally similar 15-20 kDa proteins are involved in the transport, and possibly metabolism, of these compounds. The milk protein beta-lactoglobulin B (beta-LG) is an 18 kDa protein which binds retinol and may be involved in oral delivery of retinol to neonates. beta-LG also binds drugs and other natural products and is of potential interest as a protective delivery vehicle.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0724-8741
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
651-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10350006-Binding Sites,
pubmed-meshheading:10350006-Carbon Radioisotopes,
pubmed-meshheading:10350006-Computer Simulation,
pubmed-meshheading:10350006-Cyclohexanones,
pubmed-meshheading:10350006-Lactoglobulins,
pubmed-meshheading:10350006-Ligands,
pubmed-meshheading:10350006-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10350006-Models, Chemical,
pubmed-meshheading:10350006-Norisoprenoids,
pubmed-meshheading:10350006-Protein Conformation,
pubmed-meshheading:10350006-Retinoids,
pubmed-meshheading:10350006-Terpenes
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pubmed:year |
1999
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pubmed:articleTitle |
NMR studies of retinoid-protein interactions: the conformation of [13C]-beta-ionones bound to beta-lactoglobulin B.
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pubmed:affiliation |
Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, The Ohio State University, Columbus 43210, USA. curley.1@osu.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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