Adenosinetriphosphatase activity of brain

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Abstract
ATPase of guinea pig brain homogenates showed pH optima at 7.4 and 8.2, required the presence of Mg++ and was inhibited by Ca++. CUSO4, Na iodoacetate, alloxan, NaF, and diethylbarbituric acid were active inhibitors; cyanide, 2,4-dinitrophenol, purines, barbiturate drugs, alkaloids, atropine, glucose, glutamate, creatine, thiamine, and epinephrine were inactive or poor inhibitors. Comparison indicated that the extracts contained separate enzymes for ATPase and inorganic pyrophosphatase activity.