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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
24
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pubmed:dateCreated |
1990-3-14
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pubmed:abstractText |
The photochemical and the subsequent thermal behaviors of iodopsin (Cl(-)-bound form) and N-iodopsin (iodopsin whose Cl- was replaced by NO3-) in CHAPS-phosphatidylcholine (PC) were studied by low-temperature spectrophotometry. Irradiation of the iodopsin preparation at -185 degrees C produced a photo-steady-state mixture composed of iodopsin, bathoiodopsin, and isoiodopsin. Bathoiodopsin was thermally reverted to the original iodopsin. These results were almost the same as those reported previously [Yoshizawa, T., & Wald, G. (1967) Nature 214, 566-571] in which iodopsin was extracted with 2% digitonin. Therefore, photochemical and subsequent thermal behaviors of iodopsin were independent of the detergent to solubilize iodopsin. Irradiation of N-iodopsin at -185 degrees C produced the similar photo-steady-state mixture. However, N-bathoiodopsin was thermally converted to the next intermediate, presumably N-lumiiodopsin. These results suggest that the batho-lumi transition of iodopsin at low temperature is likely to be inhibited by the Cl- bound to the protein moiety of iodopsin, while at room temperature the Cl- bound to iodopsin could be released on the conversion process of batho- to lumiiodopsin.
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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 |
Nov
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9412-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2611241-Animals,
pubmed-meshheading:2611241-Chickens,
pubmed-meshheading:2611241-Chlorides,
pubmed-meshheading:2611241-Light,
pubmed-meshheading:2611241-Retinal Pigments,
pubmed-meshheading:2611241-Rod Opsins,
pubmed-meshheading:2611241-Spectrum Analysis,
pubmed-meshheading:2611241-Temperature,
pubmed-meshheading:2611241-Thermodynamics
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pubmed:year |
1989
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pubmed:articleTitle |
Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature.
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pubmed:affiliation |
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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