Abstract
1. When Na-K ATPase [EG 3.6.1.3] preparation from guinea pig kidney cortex was preincubated with BeCl2 in the presence of Mg++, the activity was inhibited. 2. For beryllium inhibition of Na-K ATPase, Mg++ was necessary and was substituted by Mn++, but not by Ca++. 3. Beryllium chloride concentration required for 50% of Na-K ATPase activity was 1.8x10−5m. 4. In the presence of Mg++, K+ increased the rate of inhibition and was substituted by NH4+ or Rb+, but not by Li+. 5. Sodium ion not only protected the enzyme from the inhibition in the presence of K+ and Mg++, but also reversed the inhibition 6. Protective effect of Na+ was remarkable in the absence of K+ or presence of its low concentration. 7. Ouabain did not affect the rate of inhibition in the presence of K+ and Mg++

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