Abstract
Na +, K +-ATPase was isolated from calf heart. The specific activity was measured by a spectrophotometric method which allowed continual monitoring of the reaction. Ouabain-induced inhibition of the enzyme system was shown to be both temperature and time-dependent. [ 3H]Ouabain binding in the presence of ATP, Mg 2+, Na + and K + was shown to be time-dependent. A direct temporal correlation between ouabain binding and inhibition of specific activity of the enzyme system was demonstrated. The effects of K + and ouabain reinforce the allosteric nature of the Na +, K +-ATPase.
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