Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits
Author:
Publisher
American Society for Microbiology
Subject
Applied Microbiology and Biotechnology
Link
https://journals.asm.org/doi/pdf/10.1128/mr.51.4.477-497.1987
Reference143 articles.
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2. Purification and functional properties of the DCCD-reactive proteolipid subunit of the H+-translocating ATPase from Mycobacterium phlei;Agarwal N.;Biochim. Biophys. Acta,1983
3. Isolation, characterization, and reconstitution of a solubilized fraction containing the hydrophobic sector of the mitochondrial proton pump;Alfonzo M.;J. Bioenerg. Biomembr.,1981
4. Localization and nucleotide-sequence of the gene for the ATP synthase proteolipid subunit on the spinach plastid chromosome;Alt J.;Curr. Genet.,1983
5. Purification of the DCCD-reactive protein of the energy-transducing adenosine triphosphatase complex from Escherichia coli;Altendorf K.;FEBS Lett.,1977
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