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(Na+ + K+)-ATPase: on the number of the ATP sites of the functional unit

Journal of Bioenergetics and Biomembranes

Aug 1, 1987

A Askari

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Abstract

Questions concerning the number of the ATP sites of the functional unit of (Na+ + K+)-ATPase (i.e., the sodium pump) have been at the center of the controversies on the mechanisms of the catalytic and transport functions of the enzyme. When the available data pertaining to the number of...read more

Mentioned in this Paper

Macromolecular Compounds
Adenosine Triphosphatases
Sodium Pump Activity
Sodium Pump Location
Striadyne
ATP1A1
Adenosinetriphosphatase
Na(+)-K(+)-Exchanging ATPase
Paper Details
References
  • References57
  • Citations26
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  • References57
  • Citations26
123

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(Na+ + K+)-ATPase: on the number of the ATP sites of the functional unit

Journal of Bioenergetics and Biomembranes

Aug 1, 1987

A Askari

PMID: 3040699

DOI: 10.1007/bf00768539

Abstract

Questions concerning the number of the ATP sites of the functional unit of (Na+ + K+)-ATPase (i.e., the sodium pump) have been at the center of the controversies on the mechanisms of the catalytic and transport functions of the enzyme. When the available data pertaining to the number of...read more

Mentioned in this Paper

Macromolecular Compounds
Adenosine Triphosphatases
Sodium Pump Activity
Sodium Pump Location
Striadyne
ATP1A1
Adenosinetriphosphatase
Na(+)-K(+)-Exchanging ATPase

Feeds With Similar Papers

Bacterial Respiration

This feed focuses on cellular respiration in bacteria, known as bacterial respiration. Discover the latest research here.

Related Papers

Nature

Are transport proteins porous?

NatureJuly 16, 1981
N M Green
Experimental Eye Research

Vanadate stimulation of phosphotyrosine protein levels in quiescent Nakano mouse lens cells

Experimental Eye ResearchApril 1, 1987
S GentlemanT M Martensen
Paper Details
References
  • References57
  • Citations26
12345...
  • References57
  • Citations26
123

Download from

Publisher
PubMed
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