1988 Fiscal Year Final Research Report Summary
Mechanism of Na^+ pump and F^- dependent inhibition
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 |
Research Field |
Functional basic dentistry
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Research Institution | HOKKAIDO UNIVERSITY |
Principal Investigator |
KAZUYA Taniguchi Dept. Pharmacol. Sch. Dentistry, Hokkaido University, 歯学部, 助教授 (40028204)
|
Co-Investigator(Kenkyū-buntansha) |
KUNIAKI Suzuki Dept. Pharmacol. Sch. Dentistry, Hokkaido University, 歯学部, 助手 (40133748)
|
Project Period (FY) |
1986 – 1988
|
Keywords | Na^+ pump / Na^+ / k^+-ATPase / K+-ATPase |
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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Research Products
(14 results)