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Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements

Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements

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SCHWAPPACH, Blanche, Werner STÜRMER, Hans-Jürgen APELL, Steven J. D. KARLISH, 1994. Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements. In: The Journal of Biological Chemistry. 269(26), pp. 21620-21626

@article{Schwappach1994Bindi-7774, title={Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements}, year={1994}, 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.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7774"> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <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:contributor>Schwappach, Blanche</dc:contributor> <dc:format>application/pdf</dc:format> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:37:26Z</dcterms:available> <dcterms:bibliographicCitation>First publ. in: The Journal of Biological Chemistry 269 (1994), 26, pp. 21620-21626</dcterms:bibliographicCitation> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7774"/> <dcterms:title>Binding of Sodium Ions and Cardiotonic Steroids to Native and Selectively Trypsinized Na,K Pump, Detected by Charge Movements</dcterms:title> <dc:creator>Karlish, Steven J. D.</dc:creator> <dc:creator>Stürmer, Werner</dc:creator> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dc:contributor>Karlish, Steven J. D.</dc:contributor> <dc:language>eng</dc:language> <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>Stürmer, Werner</dc:contributor> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:creator>Schwappach, Blanche</dc:creator> </rdf:Description> </rdf:RDF>

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