Evidence for a new intermediate state in the mechanism of (Na+ + K+)-adenosine triphosphatase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference20 articles.
1. A Phosphorylated Intermediate in Adenosine Triphosphate-dependent Sodium and Potassium Transport across Kidney Membranes
2. Sodium-Potassium-activated Adenosine Triphosphatase of Electrophorus Electric Organ
3. Formation and Decomposition of a Phosphorylated Intermediate in the Reaction of Na+-K+ Dependent ATPase*
4. Sodium-Potassium-activated Adenosine Triphosphatase of Electrophorus Electric Organ
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1. Influence of additional metal ions on the ratio of conversion rates of intermediate products of the hydrolysis of adenosine-5′-triphosphoric acid catalyzed by the Cu2+ ion: 1. Experimental study of the influence of Mg2+ ions in the ascending branch of the dependence of the initial hydrolysis rate on pH;Russian Journal of Physical Chemistry B;2012-09
2. Influence of additional metal ions on the ratio of the rates of intermediate product transformations in the hydrolysis of adenizine-5′-triphosphoric acid catalyzed by divalent Cu ions;Russian Journal of Physical Chemistry B;2009-12
3. Evidence for Two Different Reactive Sulfhydryl Groups in the ATP-Binding Sites of (Na++ K+)-ATPase;European Journal of Biochemistry;2005-03-03
4. On the Mechanism of Activation of the Plasma Membrane Ca2+-ATPase by ATP and Acidic Phospholipids;Journal of Biological Chemistry;2003-06
5. Acid-labile ATP and/or ADP/Pi Binding to the Tetraprotomeric Form of Na/K-ATPase Accompanying Catalytic Phosphorylation-Dephosphorylation Cycle;Journal of Biological Chemistry;1999-11
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