Transient state in the phosphorylation of sodium- and potassium- transport adenosine triphosphatase by adenosine triphosphate.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. The Sodium Pump
2. The (Na+ + K+)-activated ATPase Enzymatic and transport properties
3. Two Kinds of High Energy Phosphorylated Intermediate, with and without Bound ADP, in the Reaction of Na+-K*-dependent ATPase*
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1. Equilibrium of Phosphointermediates of Sodium and Potassium Ion Transport Adenosine Triphosphatase;Journal of General Physiology;1997-05-01
2. Indicators of conformational changes in the Na+/K+-ATPase and their interpretation;Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes;1993-06
3. Chemistry and energetics of transphosphorylations in the mechanism of Na+/K+-transporting ATPase: an attempt at a unifying model;Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes;1993-06
4. K+-site-directed pyridine derivative, AU-1421, activates hydrolysis of the K+-sensitive phosphoenzyme of sarcoplasmic reticulum Ca2+-ATPase and inactivates that of K+-transporting ATPases;Biochimica et Biophysica Acta (BBA) - Biomembranes;1992-04
5. Rapid inhibition of the K+-sensitive phosphoenzyme of Na+/K+-ATPase by (Z)-5-methyl-2-[2-(1-naphthyl)ethenyl]-4-piperidinopyridine;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-06
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