The epsilon subunit of Escherichia coli coupling factor 1 is required for its binding to the cytoplasmic membrane.
Open Access
- 1 May 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (9) , 3123-3128
- https://doi.org/10.1016/s0021-9258(17)40811-8
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coliBiochemistry, 1977
- Assembly of the catalytic unit of the Escherichia coli membrane ATPase in vitro requires the γ chainBiochemistry, 1977
- Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coliBiochemistry, 1977
- Subunits of the bacterial proton-pump ATPase: A synopsisJournal of Cellular Physiology, 1976
- The role of δ subunit in the coupling activity of chloroplast coupling factor 1FEBS Letters, 1976
- Structure and function of chloroplast ATPaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1976
- ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunitsBiochemistry, 1976
- Partial purification of active delta and epsilon subunits of the membrane ATPase from escherichia coliJournal of Supramolecular Structure, 1975
- Oxidative phosphorylation and proton translocation in membrane vesicles prepared from Escherichia coliBiochemical and Biophysical Research Communications, 1974
- Properties of a soluble Ca2+- and Mg2+-activated ATPase released from Escherichia coli membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1972