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Abstract
The 2,4-dinitrophenol (DNP) stimulated ATPase activity has been studied in rat liver mitochondria which have a K + content of 15 mM or less. It has been found that in these mitochondria the ATPase activity becomes strictly dependent on K + and on electron transport. The activity reaches a maximum with 20 mM KCl and is inhibited by rotenone and antimycin. Succinate, in some experiments, enhances the DNP stimulated ATPase activity in a malonate sensitive process.
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