Heterogeneity of pig kidney Na,K-ATPase as indicated by ADP- and ouabain-binding stoichiometry
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference31 articles.
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1. Correcting binding parameters for interacting ligand-lattice systems;Physical Review E;2017-07-31
2. Preparation of Na+,K+-ATPase with Near Maximal Specific Activity and Phosphorylation Capacity: Evidence That the Reaction Mechanism Involves All of the Sites;Biochemistry;1999-05-20
3. Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function;American Journal of Physiology-Renal Physiology;1998-11-01
4. Half-site Modification of Lys-480 of the Na+,K+-ATPase α-Chain with Pyridoxal 5′-Diphospho-5′-adenosine Reduces ATP-dependent Phosphorylation Stoichiometry from Half to a Quarter;Journal of Biological Chemistry;1998-09
5. Comparative Aspects of Ligand Stoichiometry in Na+, K+-ATPase from Kidney and in Ca2+-ATPase from Rabbit Sarcoplasmic Reticulum;Annals of the New York Academy of Sciences;1997-11
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