Determination of rate constants for nucleotide dissociation from Na,K-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference18 articles.
1. Binding of Adenosine Triphosphate to Sodium and Potassium Ion-stimulated Adenosine Triphosphatase
2. Binding of ATP to brain microsomal ATPase Determination of the ATP-binding capacity and the dissociation constant of the enzyme-ATP complex as a function of K+ concentration
3. (Na+ + K+)-ATPase: confirmation of the three-pool model for the phosphointermediates of Na+-ATPase activity. Estimation of the enzyme-ATP dissociation rate constant
4. Elementary steps of the (Na+ + K+)-ATPase mechanism, studied with formycin nucleotides
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2. Anion interactions with Na,K-ATPase: simultaneous binding of nitrate and eosin;European Biophysics Journal;2004-05-15
3. Identification of Potential Regulatory Sites of the Na+,K+-ATPase by Kinetic Analysis;Biochemistry;2004-02-05
4. Quantitative Analysis of the Interaction between the Fluorescent Probe Eosin and the Na+/K+-ATPase Studied through Rb+ Occlusion;Biochemistry;2004-01-30
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