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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1996-7-15
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pubmed:abstractText |
The retinal pigment epithelium (RPE) contains an abundant opsin that is distinct from rhodopsin and cone visual pigments and is able to bind the retinaldehyde chromophore. The putative retinal G protein-coupled receptor (RGR) was isolated in digitonin solution from bovine RPE microsomes and copurified consistently with a minor 34-kDa protein. The absorption spectrum of RGR revealed endogenous pH-sensitive absorbance in the blue and near-ultraviolet regions of light. Membrane-bound RGR was incubated with exogenously added all-trans-retinal and formed two long-lived pH-dependent photopigments with absorption maxima of 469 +/- 2.4 and 370 +/- 7.3 nm. The effects of hydrogen ion concentration suggest that the blue and near-UV photopigments are tautomeric forms of RGR, in which an all-trans-retinal Schiff base is protonated or unprotonated, respectively. The RPE pigment was also demonstrable by its reactivity to hydroxylamine in the dark. The retinaldehyde-RGR conjugate at neutral pH favors the near-UV pigment and is a novel light-absorbing opsin in the vertebrate eye.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/G protein-coupled receptor RGR,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxylamine,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Retinaldehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Rod Opsins,
http://linkedlifedata.com/resource/pubmed/chemical/Schiff Bases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6251-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8639565-Animals,
pubmed-meshheading:8639565-Cattle,
pubmed-meshheading:8639565-Eye Proteins,
pubmed-meshheading:8639565-GTP-Binding Proteins,
pubmed-meshheading:8639565-Hydrogen-Ion Concentration,
pubmed-meshheading:8639565-Hydroxylamine,
pubmed-meshheading:8639565-Hydroxylamines,
pubmed-meshheading:8639565-Light,
pubmed-meshheading:8639565-Pigment Epithelium of Eye,
pubmed-meshheading:8639565-Receptors, Cell Surface,
pubmed-meshheading:8639565-Receptors, G-Protein-Coupled,
pubmed-meshheading:8639565-Retinaldehyde,
pubmed-meshheading:8639565-Rod Opsins,
pubmed-meshheading:8639565-Schiff Bases,
pubmed-meshheading:8639565-Spectrophotometry,
pubmed-meshheading:8639565-Spectrophotometry, Ultraviolet,
pubmed-meshheading:8639565-Stereoisomerism,
pubmed-meshheading:8639565-Ultraviolet Rays
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pubmed:year |
1996
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pubmed:articleTitle |
Blue and ultraviolet light-absorbing opsin from the retinal pigment epithelium.
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pubmed:affiliation |
Department of Microbiology, University of Southern California School of Medicine, Los Angeles, USA.
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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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