Phosphorylation of H2O2-treated lens Na+,K+-ATPase.
It has been previously shown that H2O2 inhibits lens 86Rb influx and results in modification of Na+,K+-ATPase with respect to ATP hydrolysis. The effect of H2O2 on ATP hydrolysis was further investigated using [gamma-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 H2O2 treatment. Similar results were observed for partially purified Na+,K+-ATPase from bovine kidney, porcine brain and canine kidney.
D000818:Animals; D001921:Brain / Q000201:enzymology; D002386:Cataract / Q000201:enzymology; D002417:Cattle; D046508:Culture Techniques; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D007668:Kidney / Q000201:enzymology; D007908:Lens, Crystalline / Q000187:drug effects / Q000201:enzymology*; D010766:Phosphorylation; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013552:Swine
D006861:Hydrogen Peroxide; D000254:Sodium-Potassium-Exchanging ATPase