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  • Title: [Regulation of Na, K-ATPase activity by monovalent cations].
    Author: Boldyrev AA, Kozlova IO, Smirnova IN, Shvets VI.
    Journal: Biokhimiia; 1977 Aug; 42(8):1466-70. PubMed ID: 20994.
    Abstract:
    A deviation from optimal conditions of the Na, K-ATPase reaction results in a drastic change in the plot: enzyme activity versus Na/K ratio. Acidification of the medium and a decrease in Mg2+ concentration and temperature results in two peaks on the curve at Na/K ratio of about 1 and at Na/K ratio greater than 4. The enhancement of pH of the medium and increase in Mg2+ concentration decreases the first peak and increases the second one. A comparison of these curves for hydrolysis of ATP, UTP and p-nitrophenylphosphate and temperature dependence of the hydrolysis of the substrates suggest that the anomalies observed may be accounted for the Na+ effect on the K-sites or K+ effect on the Na-sites under conditions when cation-binding sites are heterogeneous.
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