Effect of magnesium ions on the high-affinity binding of eosin to the (Na+ + K+)-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference14 articles.
1. 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
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3. Conformational transitions between Na+-bound and K+-bound forms of (Na+ + K+)-ATPase, studied with formycin nucleotides
4. Tryptophan fluorescence of (Na+ + K+)-ATPase as a tool for study of the enzyme mechanism
5. Effect of ATP on the intermediary steps of the reaction of the (Na++K+)-dependent enzyme system. II. Effect of a variation in the ATP/Mg2+ ratio
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1. The E2P-like state induced by magnesium fluoride complexes in the Na,K-ATPase. Kinetics of formation and interaction with Rb+;Biochimica et Biophysica Acta (BBA) - Biomembranes;2015-07
2. Fluorone dyes have binding sites on both cytoplasmic and extracellular domains of Na,K-ATPase;Biochimica et Biophysica Acta (BBA) - Biomembranes;2013-02
3. Kinetic characterization of Na,K-ATPase inhibition by Eosin;Blood Cells, Molecules, and Diseases;2007-05
4. Eosin Fluorescence Changes during Rb+ Occlusion in the Na+/K+-ATPase;Biochemistry;2006-10-01
5. TNP-8N3-ADP Photoaffinity Labeling of Two Na,K-ATPase Sequences under Separate Na+ plus K+ Control;Biochemistry;2006-02-11
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