A kinetic description for sodium and potassium effects on (Na++K+)-adenosine triphosphatase: a model for a two-nonequivalent site potassium activation and an analysis of multiequivalent site models for sodium activation

1. Dissociation constants for sodium and potassium of a site that modulates the rate of ouabain-(Na + +K + )-ATPase interaction were applied to models for potassium activation of (Na + +K + )-ATPase. The constants for potassium (0·213 m M ) and for sodium (13·7 m M ) were defined, respectively, as...

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