Acetyl phosphate as a substitute for ATP in (Na− + K+)-dependent ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference35 articles.
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2. A Phosphorylated Intermediate in Adenosine Triphosphate-dependent Sodium and Potassium Transport across Kidney Membranes
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1. ROLE OF PROTEIN CONFORMATION CHANGES AND TRANSPHOSPHORYLATIONS IN THE FUNCTION OF Na+/K+-TRANSPORTING ADENOSINE TRIPHOSPHATASE: AN ATTEMPT AT AN INTEGRATION INTO THE Na+/K+ PUMP MECHANISM;Biological Reviews;2010-09-06
2. The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site;European Journal of Biochemistry;2004-09-16
3. Characterization of K+-dependent and K+-independentp-nitrophenylphosphatase activity of synaptosomes;Neurochemical Research;1993-07
4. Phosphorylation of Na,K-ATPase by acetyl phosphate and inorganic phosphate. Sidedness of Na+, K+ and nucleotide interactions and related enzyme conformations;Biochimica et Biophysica Acta (BBA) - Biomembranes;1991-04
5. Reversible inhibition of sodium and potassium-dependent adenosine triphosphatase by the pyridine derivative, AU-1421 during turnover cycle;Biochemical Pharmacology;1990-10
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