Evidence for essential disulfide bonds in the beta-subunit of (Na+ + K+)-ATPase.
(Na+ + K+)-ATPase from dog kidney lost its activity when heated at 55 degrees C in the presence of 0.3 M 2-mercaptoethanol. Either heat treatment alone or addition of reducing agent at around 25 degrees C caused little inactivation. One disulfide bond per protomer (mol. wt. 146 000) was reduced in the inactivated sample but in active samples no reduction occurred. Neither K+-dependent phosphatase activity nor phosphoenzyme formation in the presence of Na+ was detected in the inactivated sample, suggesting that the disulfide bond was essential for the catalytic cycle of (Na+ + K+)-ATPase. This essential disulfide bond belonged to the beta-subunit, the glycoprotein component of the enzyme, indicating that the beta-subunit may be an integral component of the (Na+ + K+)-ATPase system.
D000818:Animals; D004220:Disulfides / Q000378:metabolism*; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D007679:Kidney Medulla / Q000201:enzymology; D046911:Macromolecular Substances; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D004220:Disulfides; D046911:Macromolecular Substances; D008623:Mercaptoethanol; D000254:Sodium-Potassium-Exchanging ATPase