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Conference Paper

Cation Selectivity of Membrane Proteins

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Mezele,  Martin
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Lewitzki,  Erwin
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Ruf,  Horst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Grell,  Ernst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Mezele, M., Lewitzki, E., Ruf, H., & Grell, E. (1988). Cation Selectivity of Membrane Proteins. Berichte der Bunsen-Gesellschaft, 92(9), 998-1004. doi:10.1002/bbpc.198800249.


Cite as: https://hdl.handle.net/21.11116/0000-0008-0EF9-1
Abstract
In order to investigate the high‐affinity K+ binding to proteins, alkali ion binding studies were performed on a fluorescent derivative of membrane‐bound Na,K‐ATPase in buffered aqueous solution at 37°C employing a specially designed automatic spectrofluorometric titration system. The comparison of the obtained apparent stability constants, which reached values for K+ even over 104 M−1 with those of a simpler cyclic peptide, acting as a suitable model compound, provides suggestions concerning the molecular nature of the binding sites involved.