Hydrophobic labeling of (sodium, potassium)-ATPase: further evidence that the .beta. subunit is embedded in the membrane bilayer
- 26 April 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (9), 2296-2300
- https://doi.org/10.1021/bi00278a037
Abstract
O-Hexanoyl-3,5-diido-N-(4-azido-2-nitrophenyl)tyramine was 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.This publication has 7 references indexed in Scilit:
- Hormonal regulation of (Na+,K+)-ATPase biosynthesis in the toad bladder. Effect of aldosterone and 3,5,3'-triiodo-L-thyronine.Journal of Biological Chemistry, 1982
- Evidence for the organization of the transmembrane segments of (Na,K)-ATPase based on labeling lipid-embedded and surface domains of the alpha-subunit.Journal of Biological Chemistry, 1982
- Immunochemical evidence for a transmembrane orientation of both the (sodium(1+), potassium(1+) ion-activated)-ATPase subunitsBiochemistry, 1981
- Labeling of lymphocyte surface antigens by the lipophilic, photoactivatable reagent hexanoyl diiodo-N-(4-azido-2-nitrophenyl)tyramineBiochemistry, 1980
- Identification of regions of the catalytic subunit of (Na-K)-ATPase embedded within the cell membrane. Photochemical labeling with [3H]adamantane diazirine.Journal of Biological Chemistry, 1980
- Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labeled with ATP and iodoacetateJournal of Biological Chemistry, 1979
- The lipid requirement of the (Ca2+ + Mg2+)-ATPase in the human erythrocyte membrane, as studied by various highly purified phospholipasesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977