Abstract
SummaryMeasurement of the activity of ATP-ase in salt concentrations from 0.15 to 0.55 M show that the activity is decreased as the KC1 concentration increases. The magnitude of the effect depends upon pH and the presence or absence of glycine. The rate of formation of inoranic phosphote is also found to be independent of the substrate concentration when the ATP concentration is 0.23 mM per liter or greater. Observed deviations from a linear rate of formation of phosphate at the higher ATP concentration must be attributed to inactivation of the enzyme during the course of the experiment.
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