Mechanism of lipid activation of Na, K, Mg-activated adenosine triphosphatase and K, Mg-activated phosphatase of bovine cerebral cortex

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Abstract
Na+, K+, Mg++-activated adenosine triphosphatase and K+, Mg++-activatedp-nitrophenyl phosphatase prepared from a membrane fraction of bovine cerebral cortex were studied with regard to the manner of their activation by phospholipids, using phosphatidyl serine, lysolecithin, monodecyl and didecyl phosphates. The kinetic and chromatographic studies suggested the following. (1) When the enzyme proteins bind the phospholipids in a proper ratio, they attain the optimum activation. (2) The binding causes a simple conversion of the enzymes from an inactive form to a fully activated form. (3) The lipids in both micellar form and molecular dispersion activate the enzymes. (4) Of the proteins contained in the enzyme preparation, only a group of proteins possessing the ATPase and the phosphatase activities bind phospholipids, and the amount of the bound lipids is limited.