Effects of Cations on High-Affinity and Low- Affinity ATP-Binding Sites of (Na+, K+)-ATPase as S+tudied by Disulfides of Thioinosine Triphosphate and Its Analogue
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1981.tb06449.x/fullpdf
Reference41 articles.
1. The Sodium-Potassium Adenosinetriphosphatase
2. Sodium Transport by Phospholipid Vesicles Containing Purified Sodium and Potassium Ion-activated Adenosine Triphosphatase
3. The Sodium Pump
4. Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool
5. Formation and Decomposition of a Phosphorylated Intermediate in the Reaction of Na+-K+ Dependent ATPase*
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1. Synthesis and biochemical characterization of the new sulfhydryl-reactive ATP analog 8-thiocyano-ATP. Its interaction with sodium-potassium ATPase and kinases;Biochemistry;1992-02
2. Inhibitory effects of cytotoxic disulfides on membrane Na+,K+-ATPase;Biochemical Pharmacology;1990-05
3. [28] Irreversible and reversible modification of SH groups and effect on catalytic activity;Methods in Enzymology;1988
4. (Na+ + K+)-ATPase: On the number of the ATP sites of the functional unit;Journal of Bioenergetics and Biomembranes;1987-08
5. Chromium(III)ATP inactivating (Na+ + K+)-ATPase supports Na+-Na+ and Rb+-Rb+ exchanges in everted red blood cells but not Na+,K+ transport;European Journal of Biochemistry;1986-06
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