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Kinetic and spectroscopic characterisation of the cardiac glycoside binding site of Na+/K+-ATPase employing a dansylated ouabain derivative

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

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Frank,  Ursula
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Götz,  Elisabeth
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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

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Citation

Lewitzki, E., Frank, U., Götz, E., & Grell, E. (1994). Kinetic and spectroscopic characterisation of the cardiac glycoside binding site of Na+/K+-ATPase employing a dansylated ouabain derivative. In E. Bamberg, & W. Schoner (Eds.), The Sodium Pump (pp. 625-628). Darmstadt, Germany: Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994.


Cite as: https://hdl.handle.net/21.11116/0000-0007-FDF2-B
Abstract
Fluorescence spectroscopy is a useful tool for studying equilibrium and dynamic properties related to structural aspects of biological systems. Dansylated compounds have been widely used as fluorescent probes to characterize protein structure. Their wide use is a result of a favourable lifetime (~10 nsec), promising spectral characteristics, including the high sensitivity of the emission spectrum of the dansyl moiety to solvent polarity, and suitability for energy transfer studies with tryptophan residues in proteins