COMPARISON OF LIPID EFFECTS ON K+-MG2+ ACTIVATED P-NITROPHENYL PHOSPHATASE AND NA+-K+-MG2+ ACTIVATED ADENOSINE TRIPHOSPHATASE OF MEMBRANE

Abstract— A comparison was made between K+‐Mg2+ activated p‐nitrophenyl phosphatase and Na+‐K+‐Mg2+ activated adenosine triphosphatase with a solubilized enzyme preparation from a membrane fraction of cerebral cortex. The NPPase showed activity even in the absence of phospholipid, whereas the ATPase required the lipid for its activity. More varied types of phospholipids were effective in activating the NPPase than the ATPase, and with each phospholipid the extent and the pattern of the NPPase activation differed from that of the ATPase. By deoxycholate treatment the pH optimum of the NPPase was shifted independently from the pH optimum shift of the ATPase. The specific activity ratio of the NPPase to the ATPase was not constant during purification. These two enzymes were, however, not separable with ammonium sulphate fractionation, and their thermo‐lability was identical regardless of the presence of phospholipid. The results suggested two possibilities: (1) the NPPase is a separate enzyme entity from the ATPase; (2) although the NPPase is a part of the ATPase system, the mechanism of action of lipids on the former part differs from that on the rest of the system. Copyright © 1969, Wiley Blackwell. All rights reserved