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1. A study has been made to see whether the ATPase of the Na pump is activated by phospholipids.

2. Solubilization of a membrane-containing (microsomal) fraction from ox brain cortex with deoxycholate removed most or all of the ouabain-inhibited ATPase and p-nitrophenylphosphatase (pNPPase) activities. Addition of sonicated dispersions of crude commercial samples of phosphatidic acid, phosphatidylinositol or phosphatidylserine stimulated both enzymic activities, but neither phosphatidylcholine nor phosphatidylethanolamine affected them. After partial purification by chromatography, however, definite activation was demonstrated only with that component of crude samples which migrated like phosphatidylserine.

3. The ATPase activity dependent on phosphatidylserine was eliminated by removal of Na and K or by addition of ouabain and was substantially inhibited by oligomycin. The corresponding component of pNPPase activity was partially inhibited by ouabain or by removal of most of the K, but was little affected by oligomycin. The phosphatidylserine-dependent enzyme(s) therefore exhibited properties characteristic of the ATPase of the Na pump.

4. Phosphatidylserine dispersions similarly activated both the ATPase and the pNPPase of the particulate enzyme preparations, untreated with deoxycholate.

5. The results suggest that the system for active transport of Na and K involves a complex unit of phosphatidylserine and the protein of the ATPase.