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F0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c.
Steffens K, Hoppe J, Altendorf K. Steffens K, et al. Among authors: altendorf k. Eur J Biochem. 1988 Jan 4;170(3):627-30. doi: 10.1111/j.1432-1033.1988.tb13743.x. Eur J Biochem. 1988. PMID: 2892677 Free article.
Only liposomes containing intact F0 or all subunits of F0 were active in proton translocation and F1 binding [Schneider, E. and Altendorf, K. (1985) EMBO J. 4, 515-518]. The conformation of subunit c in the different preparations was analyzed by labelling the proteo …
Only liposomes containing intact F0 or all subunits of F0 were active in proton translocation and F1 binding [Schneider, E. and Altendorf
Fo portion of Escherichia coli ATP synthase. Further resolution of trypsin-generated fragments from subunit b.
Steffens K, Schneider E, Deckers-Hebestreit G, Altendorf K. Steffens K, et al. Among authors: altendorf k. J Biol Chem. 1987 Apr 25;262(12):5866-9. J Biol Chem. 1987. PMID: 2883181 Free article.
Labeling of isolated trypsin-treated Fo fractions with the thiol-specific reagent N-(7-dimethylamino-4-methylcoumarinyl)-maleimide, which has been demonstrated recently to specifically modify subunit b (Schneider, E., and Altendorf, K. (1985) Eur. J. Biochem. 153, 1 …
Labeling of isolated trypsin-treated Fo fractions with the thiol-specific reagent N-(7-dimethylamino-4-methylcoumarinyl)-maleimide, which ha …
187 results