| Project/Area Number |
61480381
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Functional basic dentistry
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| Research Institution | HOKKAIDO UNIVERSITY |
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Principal Investigator |
KAZUYA Taniguchi Dept. Pharmacol. Sch. Dentistry, Hokkaido University, 歯学部, 助教授 (40028204)
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| Co-Investigator(Kenkyū-buntansha) |
KUNIAKI Suzuki Dept. Pharmacol. Sch. Dentistry, Hokkaido University, 歯学部, 助手 (40133748)
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| Project Period (FY) |
1986 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥5,500,000 (Direct Cost: ¥5,500,000)
Fiscal Year 1988: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1987: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1986: ¥3,500,000 (Direct Cost: ¥3,500,000)
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| Keywords | Na^+ pump / Na^+ / k^+-ATPase / K+-ATPase / K^+-ATPase / 構造変化 / 内因性阻害物質 / 【Na^+】ポンプ |
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| Research Abstract |
Following results were obtained
1,An F^-dependent Na^+ pump inhibitor which inhibits ATP binding to the Na^+ pump was registant to acid and proteolysis but labile babill to alkaline.
2,ATP did no bind to E_1P in such a way as to accelerate the breakdown of the phosphoenzyme
3,The site of attachment of BIPM probe was shown to be Cys 964 of the -chain of Na^+ pump.
4,Changes in fluorescence energy transfer between sulfhydyl fluorescence probes occured out of phase, which showed dynamic conformational changes during active transport of Na^+ and K^+.
5,Binding of Mg^<2+>, Na^+ and ATP to Na^+ pump induced the conformational change. Na^+ occlusion by oligomycin also induced the similar change. These data strongly suggest that the role of Mg ATP is to occlude Na^+.
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