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Change of inhibitor sensitivities of Escherichia coli F1-ATPase due to a mutational substitution of Phe for Ser at residue 174 of the beta subunit.
Takeda K, Miki J, Kanazawa H, Tsuchiya T, Futai M. Takeda K, et al. Among authors: futai m. J Biochem. 1985 May;97(5):1401-7. doi: 10.1093/oxfordjournals.jbchem.a135194. J Biochem. 1985. PMID: 2863263 Free article.
The F1-ATPase from the uncD11 mutant of E. coli (Kanazawa, H., Horiuchi, Y., Takagi, M., Ishino, Y., & Futai, M. (1980) J. Biochem. 88, 695-703), showed different enzymological properties from the wild-type enzyme. ...The fact that the Mg2+- and Ca2+-depe …
The F1-ATPase from the uncD11 mutant of E. coli (Kanazawa, H., Horiuchi, Y., Takagi, M., Ishino, Y., & Futai, M. (1 …
Intracistronic mapping of the defective site and the biochemical properties of beta subunit mutants of Escherichia coli H+-ATPase: correlation of structural domains with functions of the beta subunit.
Kanazawa H, Noumi T, Oka N, Futai M. Kanazawa H, et al. Among authors: futai m. Arch Biochem Biophys. 1983 Dec;227(2):596-608. doi: 10.1016/0003-9861(83)90489-7. Arch Biochem Biophys. 1983. PMID: 6320730
F1 was purified as a single complex from KF43 in this study and from KF11 previously (H. Kanazawa, Y. Horiuchi, M. Takagi, Y. Ishino, and M. Futai (1980) J. Biochem. 88, 695-703). Reconstitution experiments in vitro showed that the F1's of both mutants were d …
F1 was purified as a single complex from KF43 in this study and from KF11 previously (H. Kanazawa, Y. Horiuchi, M. Takagi, Y. Ishino, …
299 results