Abstract
It has been previously shown that H 2O 2 inhibits lens 86Rb influx and results in modification of Na +,K +-ATPase with respect to ATP hydrolysis. The effect of H 2O 2 on ATP hydrolysis was further investigated using [γ- 32P]-ATP to examine the Na +,K +-ATPase phosphorylated intermediate. A Na +-dependent phosphorylated polypeptide with an apparent molecular weight of approximately 100 000 was detected in all lens preparations, irrespective of H 2O 2 treatment. Similar results were observed for partially purified Na +,K +-ATPase from bovine kidney, porcine brain and canine kidney.
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