Regulation of the number of k-binding sites of Na,K-ATPase by adenosine triphosphate

A possible existence of two functional states of Na,K-ATPase with different electrogenic coefficients has been experimentally proved. Regulation of electrogenicity is achieved by alteration in the number of K+ transport sites. A transition of Na,K-ATPase from one functional state to the other has be...

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Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 48; no. 7; p. 1074
Main Authors Kikvidze, Z Ia, Vekua, M G, Kometiani, Z P
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.07.1983
Subjects
Adenosine Triphosphate - metabolism
Adenosine Triphosphate - pharmacology
Animals
Brain - enzymology
Kinetics
Potassium - metabolism
Protein Binding
Rats
Sodium-Potassium-Exchanging ATPase - metabolism
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Summary:A possible existence of two functional states of Na,K-ATPase with different electrogenic coefficients has been experimentally proved. Regulation of electrogenicity is achieved by alteration in the number of K+ transport sites. A transition of Na,K-ATPase from one functional state to the other has been shown to occur during the binding of ATP free ions.
ISSN:0320-9725