Dynamic lipid-protein stoichiometry on E1 and E2 conformations of the Na+/K+ -ATPase

Annular lipid-protein stoichiometry in native pig kidney Na+/K+ -ATPase preparation was studied by [125I]TID-PC/16 labeling. Our data indicate that the transmembrane domain of the Na+/K+ -ATPase in the E1 state is less exposed to the lipids than in E2, i.e., the conformational transitions are accomp...

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Bibliographic Details
Published in:FEBS letters 2011-04, Vol.585 (8), p.1153-1157
Main Authors: Mangialavori, Irene, Montes, Mónica R, Rossi, Rolando C, Fedosova, Natalya U, Rossi, Jean Paul F C
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Kidney - enzymology
Lipids - chemistry
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Protein Conformation
Sodium-Potassium-Exchanging ATPase - chemistry
Sodium-Potassium-Exchanging ATPase - metabolism
Swine
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Summary:Annular lipid-protein stoichiometry in native pig kidney Na+/K+ -ATPase preparation was studied by [125I]TID-PC/16 labeling. Our data indicate that the transmembrane domain of the Na+/K+ -ATPase in the E1 state is less exposed to the lipids than in E2, i.e., the conformational transitions are accompanied by changes in the number of annular lipids but not in the affinity of these lipids for the protein. The lipid-protein stoichiometry was 23 ± 2 (α subunit) and 5.0 ± 0.4 (β subunit) in the E1 conformation and 32 ± 2 (α subunit) and 7 ± 1 (β subunit) in the E2 conformation.
ISSN:1873-3468
DOI:10.1016/j.febslet.2011.03.024