The K+-acetylphosphatase and K+-p-nitrophenylphosphatase activities in the fraction of brain microsomes were studied as affected by anionic (sodium desoxycholate and sodium dodecyl sulphate) and nonionic (triton X-100 and digitonin) surface-active substances. The most activating concentrations of these substances are determined and their similarity with those for Na+, K+-ATPase is marked. According to the character of the effect on the K+-phosphatase and Na+, K+-ATPase activities, the studied surface-active substances are grouped on the basis of the molecule configurations, rather than ionogenic factor. Their activating effect is supposed to result from an increase in the number of functioning catalytic centres rather than the molecular activity of the enzyme. It is shown that the digitonin high concentrations may completely inhibit the Na+, K+-ATPase activity and to some extent retain the K+-acetylphosphatase activity.
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