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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
35
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pubmed:dateCreated |
1997-10-2
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pubmed:abstractText |
The bovine opsin apoprotein activates transducin, although at a much reduced level than light-activated rhodopsin (Surya, A., Foster, K., and Knox, B. (1995) J. Biol. Chem. 270, 5024-5031). The ability of retinal to modulate opsin apoprotein activity was investigated using a guanyl nucleotide exchange assay on transducin. 11-cis-Retinal reacted with opsin at 22 degrees C to (a) reform pigment having maximal absorbance at 500 nm and (b) reduce opsin activity by >80%. Pigment formation also occurred at 0 degrees C with a t1/2 of 260 min. However, unlike rhodopsin formed at 22 degrees C (R22), the rhodopsin formed at 0 degrees C (R0) activated transducin with the same half-saturating concentration as opsin in an exhaustive binding assay. Thus, the formation of a protonated Schiff base associated with 500 nm absorbance does not by itself lead to the inactivation of opsin. The R0 conformation was partially inactivated by incubation at 22 degrees C (t1/2 = 61 +/- 9 min), suggesting that it may be an intermediate conformation in the regeneration of rhodopsin.
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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/Retinaldehyde,
http://linkedlifedata.com/resource/pubmed/chemical/Rhodopsin,
http://linkedlifedata.com/resource/pubmed/chemical/Rod Opsins,
http://linkedlifedata.com/resource/pubmed/chemical/Schiff Bases,
http://linkedlifedata.com/resource/pubmed/chemical/Transducin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21745-50
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9268303-Animals,
pubmed-meshheading:9268303-Cattle,
pubmed-meshheading:9268303-Cold Temperature,
pubmed-meshheading:9268303-Darkness,
pubmed-meshheading:9268303-Hydrogen-Ion Concentration,
pubmed-meshheading:9268303-Kinetics,
pubmed-meshheading:9268303-Retinaldehyde,
pubmed-meshheading:9268303-Rhodopsin,
pubmed-meshheading:9268303-Rod Cell Outer Segment,
pubmed-meshheading:9268303-Rod Opsins,
pubmed-meshheading:9268303-Schiff Bases,
pubmed-meshheading:9268303-Transducin
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pubmed:year |
1997
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pubmed:articleTitle |
Modulation of opsin apoprotein activity by retinal. Dark activity of rhodopsin formed at low temperature.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, SUNY Health Science Center at Syracuse, Syracuse, New York 13210, USA. arjun_surya-1@sbphrd.com
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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