A mechanism of K-insensitive, ouabain-dependent liberation of Na+ from the cell during an increase in ADP intracellular concentration is studied. It is shown that the increase in the ADP/ATP ratio does not change the Na+, K+-ATPase affinity to K+ ions and does not result in the Na-activated, K-independent ATPase reaction. ADP protects ATPase from the inhibition by ouabain which is accounted for by a decrease in the concentration of a glycoside-sensitive form of the enzyme E2-P due to a turnover of the phosphokinase step of the reaction, but not due to the binding of free Mg2+ ions. The results obtained suggest that the increase in ADP concentration within the cell activates Na-Nan exchange along Na-transporting channels of the ionic pump.

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