Kinetic Studies on Na+/K+-ATPase by Using Thermokinetic Method
Author:
Publisher
Wiley
Subject
General Chemistry
Reference18 articles.
1. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain I. Substrate identity
2. Kinetic studies of membrane (NA+-K+-Mg2+)-ATPase
3. Nucleotide and divalent cation interactions with the ()-dependent ATPase
4. Substrate sites of the (Na+ + K+)-dependent ATPase
5. Kinetic Studies on a Brain Microsomal Adenosine Triphosphatase. Evidence Suggesting Conformational Changes*
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1. Investigation of the enzymatic activity of the Na+,K+-ATPase via isothermal titration microcalorimetry;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2010-08
2. Thermodynamics of Enzyme-Catalyzed Reactions: Part 7—2007 Update;Journal of Physical and Chemical Reference Data;2007-12
3. Microcalorimetric Study of Energy Metabolism of HSV-2 and FMDV Infection Processes;Chinese Journal of Chemistry;2006-02
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