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 activation constant, Ka and inhibitory constant, Ki.

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