Multiple ion-dependent and substrate-dependent sodium/potassium ATPase conformational states. Transient and steady-state kinetic studies
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00345a010
Reference50 articles.
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5. [66] Pyruvate kinase from muscle
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1. Phosphatase activity and potassium transport in liposomes with Na+, K+-ATPase incorporated;Biochimica et Biophysica Acta (BBA) - Biomembranes;1992-01
2. Phosphorylation of Na,K-ATPase by acetyl phosphate and inorganic phosphate. Sidedness of Na+, K+ and nucleotide interactions and related enzyme conformations;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-04
3. Phosphatase activity of Na+/K+-ATPase. Enzyme conformation from ligands interactions and Rb occlusion experiments;Biochimica et Biophysica Acta (BBA) - Biomembranes;1988-05
4. Substrate sites of the (Na+ + K+)-ATPase: Pertinence of the adenine and fluorescein binding sites;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1988
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