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Biological Chemistry, Graduate School of Science, Hokkaido University | 論文
- Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase α-Subunit in Mammalian Stomach Cells
- ATP-Induced Dynamic Fluorescence Changes of a N - [ p- (2-Benzimidazolyl)Phenyl] maleimide Probe at Cys^ in the α-Chain of Pig Stomach H^+, K^+-ATPase^1
- Fluorescein 5'-Isothiocyanate-Modified Na^+, K^+-ATPase, at Lys-501 of the α-Chain, Accepts ATP Independent of Pyridoxal 5'-Diphospho-5'-Adenosine Modification at Lys-480^1
- Membrane Enzyme Systems Responsible for the Ca^ - Dependent Phosphorylation of Ser^, the Independent Phosphorylation of Tyr^ and Tyr^7, and the Dephosphorylation of These Phosphorylated Residues in the α-Chain of H/K - ATPase
- Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase .ALPHA.-Subunit in Mammalian Stomach Cells.