| Project/Area Number |
63065002
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| Research Category |
Grant-in-Aid for Specially Promoted Research
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| Allocation Type | Single-year Grants |
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| Research Institution | Kyoto University |
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Principal Investigator |
YOSHIZAWA Toru Kyoto Univ., Fac. of Sci., Professor, 理学部, 教授 (10028128)
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| Co-Investigator(Kenkyū-buntansha) |
FUKUDA Yoshitaka Kyoto Univ., Fac. of Sci., Instructor, 理学部, 助手 (80165258)
SHICHIDA Yoshinori Kyoto Univ., Fac. of Sci., Instructor, 理学部, 助手 (60127090)
MAEDA Akio Kyoto Univ., Fac. of Sci., Associate Professor, 理学部, 助教授 (20012370)
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| Project Period (FY) |
1988 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥190,000,000 (Direct Cost: ¥190,000,000)
Fiscal Year 1990: ¥20,000,000 (Direct Cost: ¥20,000,000)
Fiscal Year 1989: ¥77,000,000 (Direct Cost: ¥77,000,000)
Fiscal Year 1988: ¥93,000,000 (Direct Cost: ¥93,000,000)
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| Keywords | Photoreceptor Cells / Rhodopsin / Iodopsin / GTP-Binding Protein / Laser Flash Photolysis / Low Temperature Spectrophotometry / FTIR Spectroscopy / Amino Acid Sequence / レーザー閃光分解 / 好塩菌 / レーザー閃光分解法 / 単クローン抗体 |
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| Research Abstract |
Following progresses have been made. [1] Resonance Raman spectroscopic study on 7, 9-dicis-rhodopsin demonstrated that the Schiff base linkage between its chromophore (7, 9-dicis-retinal) and bovine opsin retained anti form as in the case of rhodopsin. [2] A comparison of photoreactions between rhodopsin and 7-cis-rhodopsin revealed that an interaction between opsin and the 9-methylgroup of the chromophore changed during the lumiーmeta I transition. [3] Analysis of the photoreactions of synthetic rhodopsin analogs indicated that a conformational change around betaーionone ring of the chromophore should occur during bathoーlumi transition. [4] Laser flash photolysis of 8-memberedーrhodopsin showed that photoーbatho transition process corresponded to a relaxing pathway of highly twisted conformation of trans C_<11>-C_<12> double bond in the chromophore. [5] FTIR spectroscopy showed that the Schiff base of hypsorhodopsin was protonated. [6] In the photocycle of bacteriorhodopsin, an increase o
… More
f interaction between the protein moiety and the protonated Schiff base of the retinylidene chromophore was observed at the stages of both L and N intermediates by FTIR spectroscopy. [7] FTIR spectroscopy showed that Asp-96 in N intermediated of bacteriorhodopsin was deprotonated while Asp-85 was protonated. [8] Chromophore extraction experiments indicated that the photobleaching of iodopsin was initiated by the cis-trans isomerization of C_<11>-C_<12> double bond in the retinylidene chromophore. [9] It was suggested that the lifetime of metaiodopsin II would be extremely shorter than that of metarhodopsin II. [10] Analysis of epitope (s) of our monoclonal antibodies specific for iodopsin is now being investigated. The C-terminal part of iodopsin could be the antigenic ite. [11] A photobleaching intermediate of iodopsin was phosphorylated by purified bovine rhodopsin kinase. [12] A candidate protein for putative cone-specific G-protein alpha-subunit was partially purified from chicken retinas. [13] Amino acid sequence of iodopsin was deduced from its complementary DNA. Cloning of the other cone pigments in a chicken retina is now under progress. Less
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