The β subunit of the Escherichia coli ATP synthase exhibits a tight membrane binding property
- 1 April 1985
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 128 (1) , 155-162
- https://doi.org/10.1016/0006-291x(85)91658-4
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Oxidative phosphorylation in Escherichia coli. Characterization of mutant strains in which F1-ATPase contains abnormal β-subunitsBiochemical Journal, 1983
- STRUCTURE AND FUNCTION OF H+‐ATPase: WHAT WE HAVE LEARNED FROM Escherichia coli H+‐ATPase*Annals of the New York Academy of Sciences, 1982
- ATP Synthetase (F1F0) of Escherichia coli K‐12European Journal of Biochemistry, 1982
- Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coliBiochemical and Biophysical Research Communications, 1982
- The isolated of F0 of escherichia coli ATP‐synthase is reconstitutively active in H+‐conduction and ATP‐dependent energy‐transductionFEBS Letters, 1981
- Binding of the Ca2+, Mg2+-activated adenosine triphosphatase of Escherichia coli to phospholipid vesiclesCanadian Journal of Biochemistry, 1978
- Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coliBiochemistry, 1977