Kinetics of Na+-ATPase: influence of Na+ and K+ on substrate binding and hydrolysis
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference39 articles.
1. Sodium Ion Discharge from Pig Kidney Na+, K+-ATPase Na+-Dependency of the E1P⇌E2P Equilibrium in the Absence of KCl1
2. Transient state in the phosphorylation of sodium- and potassium- transport adenosine triphosphatase by adenosine triphosphate.
3. Kinetics of Na-ATPase activity by the Na,K pump. Interactions of the phosphorylated intermediates with Na+, Tris+, and K+.
4. Biochemical Aspects of Active Transport
5. Activation by Adenosine Triphosphate in the Phosphorylation Kinetics of Sodium and Potassium Ion Transport Adenosine Triphosphatase
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1. The interaction of Na+, K+, and phosphate with the gastric H,K-ATPase. Kinetics of E1–E2 conformational changes assessed by eosin fluorescence measurements;Biochimica et Biophysica Acta (BBA) - Biomembranes;2021-01
2. Steady-state analysis of enzymes with non-Michaelis-Menten kinetics: The transport mechanism of Na+/K+-ATPase;Journal of Biological Chemistry;2018-01
3. Alternative cycling modes of the Na+/K+-ATPase in the presence of either Na+ or Rb+;Biochimica et Biophysica Acta (BBA) - Biomembranes;2013-05
4. The crustacean gill (Na+,K+)-ATPase: Allosteric modulation of high- and low-affinity ATP-binding sites by sodium and potassium;Archives of Biochemistry and Biophysics;2008-11
5. Relationship between Ouabain-Sensitive ATPase Activity and Occluded Rb+at Micromolar ATP Concentrations;Annals of the New York Academy of Sciences;1997-11
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