Formation and decomposition of a phosphorylated intermediate in the reaction of Na+-K+ dependent ATPase

TL;DR: It was concluded that adenosine triphosphate was activating the enzyme in a fashion functionally distinct from its action as a phosphate donor, since the concentration of adenosines triph phosphate required for activation was much higher than that required for phosphorylation.

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Journal ArticleDOI

The (Na+ + K+)-activated ATPase. Enzymatic and transport properties.

Joseph D. Robinson, +1 more

- 17 Aug 1979 -

Biochimica et Biophysica Acta

Journal ArticleDOI

Binding of Adenosine Triphosphate to Sodium and Potassium Ion-stimulated Adenosine Triphosphatase

C. Hegyvary, +1 more

- 10 Sep 1971 -

Journal of Biological Chemistry

TL;DR: Binding was stable between pH 5.6 and 7.6, but declined sharply above pH 8.0, and in the presence of potassium ion alone, there appeared to be one or more binding sites on this enzyme with a much lower affinity for adenosine triphosphate.

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Journal ArticleDOI

Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site.

Steven J.D. Karlish

- 01 Aug 1980 -

Journal of Bioenergetics and Biomembrane...

TL;DR: The collected data support and extend the previous suggestion that K+ ions bound initially at a low-affinity site in state E1 are trapped in the occluded form E2· (K) by the conformational change poised far (Kc≈1000) in the direction of E2 · (K).

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Book ChapterDOI

The Na+, K+-Transporting Adenosine Triphosphatase

I. M. Glynn

TL;DR: The Na+-transporting adenosine triphosphatase (Na+,K+-ATPase), also often known as the sodium pump or sodium-potassium pump, is an enzyme that uses energy from the hydrolysis of intracellular ATP to transport Na+ ions outwards and K+ ions inwards.

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