The isolated gamma subunit of Escherichia coli F1 ATPase binds the epsilon subunit.
Open Access
- 1 July 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (13), 7354-7359
- https://doi.org/10.1016/s0021-9258(18)34384-9
Abstract
No abstract availableThis publication has 36 references indexed in Scilit:
- A Cross‐Linking Study of the Ca2+, Mg2+‐Activated Adenosine Triphosphatase of Escherichia coliEuropean Journal of Biochemistry, 1980
- Characterization of the inhibitory (.epsilon.) subunit of the proton-translocating adenosine triphosphatase from Escherichia coliBiochemistry, 1980
- Reconstitution of ATPase activity from the isolated α, β, and γ subunits of the coupling factor, F1, of Escherichia coliBiochemical and Biophysical Research Communications, 1977
- Assembly of the catalytic unit of the Escherichia coli membrane ATPase in vitro requires the γ chainBiochemistry, 1977
- Cross-linking of minor subunits in Ca2+, Mg2+-activated ATPase of escherichia coliBiochemical and Biophysical Research Communications, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Studies of substructure and tightly bound nucleotide in bacterial membrane ATPaseJournal of Supramolecular Structure, 1975
- Analytical ultracentrifugation with absorption optics and a scanner-computer system. Applications to molecular weight measurements on interacting systemsBiochemistry, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins in concentrated aqueous cesium chloride and guanidine hydrochlorideJournal of the American Chemical Society, 1967