Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coli
- 6 September 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (18), 4020-4025
- https://doi.org/10.1021/bi00637a013
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- Chymotryptic conversion of bacterial membrane ATPase to an active form with modified .alpha. chains and defective membrane binding propertiesBiochemistry, 1976
- Chemical cross-linking studies of chloroplast coupling factor 1.Journal of Biological Chemistry, 1976
- Cross-linking of minor subunits in Ca2+, Mg2+-activated ATPase of escherichia coliBiochemical and Biophysical Research Communications, 1976
- Role of Mg2+ ions in the subunit structure and membrane binding properties of bacterial energy transducing ATPaseBiochemical and Biophysical Research Communications, 1976