Hydrophobic labeling of (Na+,K+)-ATPase: further evidence that the beta subunit is embedded in the membrane bilayer.
O-Hexanoyl-3,5-diiodo-N-(4-azido-2-nitro-phenyl)tyramine has been used after photochemical conversion into the reactive nitrene to label (Na+,K+)-ATPase from Bufo marinus toad kidney. Immunochemical evidence indicates that the reagent labels both subunits of the enzyme in partially purified form as well as in microsomal membranes. These results support the view that the glycoprotein subunit, like the catalytic subunit, possesses hydrophobic domains by which it is integrated into the plasma membrane.
D000818:Animals; D002024:Bufo marinus; D007202:Indicators and Reagents / Q000494:pharmacology*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008861:Microsomes / Q000201:enzymology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D014439:Tyramine / Q000031:analogs & derivatives* / Q000494:pharmacology
D007202:Indicators and Reagents; D008051:Lipid Bilayers; D046911:Macromolecular Substances; C026227:hexanoyldiiodo-N-(4-azido-2-nitrophenyl)tyramine; D000254:Sodium-Potassium-Exchanging ATPase; D014439:Tyramine