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Na,K-ATPase on a waveguide sensor : supramolecular assembly and side directed binding studies by surface-confined fluorescence

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Grell,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Schick,  Eginhard
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Lewitzki,  Erwin
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Grell, E., Pawlak, M., Anselmetti, D., Schick, E., Lewitzki, E., & Ehrat, M. (2000). Na,K-ATPase on a waveguide sensor: supramolecular assembly and side directed binding studies by surface-confined fluorescence. In K. Taniguchi, & S. Kaya (Eds.), Na/K-ATPase and related ATPases Excerpta Medica international congress series (pp. 437-440). Amsterdam, Tokyo: Elsevier.


Cite as: https://hdl.handle.net/21.11116/0000-0008-38FA-0
Abstract
The functional assembly of FITC-Na,K-ATPase membrane fragments on a surface-modified
Ta205 waveguide allows to investigate the directed binding of ligands by surface-confined fluorescence studies. The results allow to draw conclusions about the sidedness of interactions. The fluorescence intensity decrease observed upon the selective binding of K+ is attributed to its coordination to a site ccessible from the former intracellular membrane side.