Preparation and Properties of Purified (Na+ + K+)-Stimulated Mitochondrial ATPase from Germinating Pea Seeds

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Abstract
An ATPase preparation from pea cotyledon mitochondria was purified by protamine sulfate, ammonium sulfate precipitations, and preparative gel electrophoresis. The ATPase activity was dependent upon Mg2+ and stimulated by Na+ + K+. The optimum pH of the enzyme was 8.0. A ratio of 5 to 1 between Na+ and K+ must be maintained to show maximum ATPase activity. Although no detectable amounts of phospholipids were found to be associated with the purified enzyme, it was activated by Na+ and K+ ions. Addition of phosphatidylserme and phosphatidylinositol resulted in increased activity of the (Na+ + K+)-stimulated enzyme, suggesting that the purified enzyme has probably lost most of the membrane complement during purification.

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