Na
+/K
+-ATPase, which is present in animal cell membranes, actively transports Na
+ from the inside to the outside of cell, contrary to K
+ in the reverse direction using the energy derived from the ATP hydrolysis. Oligomycin increases the affinity for Na
+ of the ATPase but not the affinity for K
+. This antibiotic inhibits the Na
+ transport but little inhibits the K
+ transport by Na
+/K
+-ATPase. In addition, this antibiotic inhibits Na
+/K
+-ATPase activity without clear effects on the partial reactions of the ATPase, which are the Na
+-dependent phosphorylation and the K
+-dependent dephosphorylation. The addition of Na
+ and oligomycin stimulates the high-affinity K
+-dependent dephosphorylation. The inhibitor of the type such as oligomycin is not known elsewhere. The study on the inhibition mechanism of oligomycin should contribute to elucidate the ion transport mechanism by Na
+/K
+-ATPase. In this paper, I review the interaction of oligomycin with Na
+/K
+-ATPase.
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