@article{Schwappach1994Bindi-7774,
  year={1994},
  title={Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements},
  number={26},
  volume={269},
  journal={The Journal of Biological Chemistry},
  pages={21620--21626},
  author={Schwappach, Blanche and Stürmer, Werner and Apell, Hans-Jürgen and Karlish, Steven J. D.}
}

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    <dc:creator>Apell, Hans-Jürgen</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: The Journal of Biological Chemistry 269 (1994), 26,  pp. 21620-21626</dcterms:bibliographicCitation>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:37:26Z</dc:date>
    <dcterms:issued>1994</dcterms:issued>
    <dc:contributor>Karlish, Steven J. D.</dc:contributor>
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    <dc:contributor>Schwappach, Blanche</dc:contributor>
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    <dcterms:title>Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements</dcterms:title>
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    <dc:creator>Karlish, Steven J. D.</dc:creator>
    <dcterms:abstract xml:lang="eng">A fluorescent dye, RH421, has been used to characterize charge movements associated with cation and cardiotonic steroid binding to Na,K-ATPase and to a specifically trypsinized preparation, so-called "19-kDa membranes." A fluorescence decrease induced by Na+ is attributed to electrogenic binding of one Na+ ion from the cytoplasm. The apparent affinity for Na+ is the same in both preparations. (ATP + Na + Mg) or (Pi + Mg)-induced fluorescence signals observed with native enzyme are not observed in 19-kDa membranes, consistent with loss of ATP binding and phosphorylation. Cardiotonic steroids (CS) bind to native enzyme and 19-kDa membranes as judged by RH421 signals, fluorescence of anthroyl ouabain, anidn hibition of Rb+ occlusion. Binding affinities to both preparations are in the micromolar range, and bindingis prevented by the presence of Na+ or K+. The kinetics of glycone binding and dissociation are identical in both preparations, but aglycones bind and dissociate about 6-foldf aster to 19-kDa membranes. Binding of Na+ and cardiotonic steroids is inactivated upon heating or extensive Pronase digestion of 19-kDa membranes. This suggests that cation and CS binding depend on the structural integrity of a complex of the proteolytic fragments, and that sites for both cations or CS consist of ligating groups located on more than one fragments of 19-kDa membranes.</dcterms:abstract>
    <dc:creator>Stürmer, Werner</dc:creator>
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