The frequency-domain method reveals the dimeric structure of Na,K-ATPase |
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Authors: | Evžen Amler Roberto Staffolani Arnošt Kotyk |
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Affiliation: | (1) Institute of Physiology, Czech Academy of Sciences, Vídeská 1083, 142 20 Prague 4, Czech Republic;(2) Institute of Biochemistry, University of Ancona, 601 00 Ancona, Italy |
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Abstract: | Lucifer yellow and lissamine rhodamine sulfonyl hydrazine were used as the donor and the receptor, respectively, for Förster energy transfer measurements to determine the location of the subunit in the native Na,K-ATPase from pig kidney. It was found that (1) the subunits are located in one functional complex, i.e., the dimer ()2 appears to be the functional complex of Na,K-ATPase, and (2) the subunits in the functional enzyme complex in the membrane are not located next to each other but are rather well separated. The distance between fluorophores covalently attached to the subunits was found to be 5.3 nm. |
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Keywords: | Na,K-ATPase frequency domain Lucifer yellow lissamine rhodamine sulfonylhydrazine dimeric structure |
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