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Electrogenic partial reactions of the SR-Ca-ATPase investigated by a fluorescence method

Electrogenic partial reactions of the SR-Ca-ATPase investigated by a fluorescence method


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BUTSCHER, Christine, Milena ROUDNA, Hans-Jürgen APELL, 1999. Electrogenic partial reactions of the SR-Ca-ATPase investigated by a fluorescence method. In: Journal of Membrane Biology. 168(2), pp. 169-181. ISSN 0022-2631. eISSN 1432-1424

@article{Butscher1999Elect-6520, title={Electrogenic partial reactions of the SR-Ca-ATPase investigated by a fluorescence method}, year={1999}, doi={10.1007/s002329900507}, number={2}, volume={168}, issn={0022-2631}, journal={Journal of Membrane Biology}, pages={169--181}, author={Butscher, Christine and Roudna, Milena and Apell, Hans-Jürgen} }

<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/123456789/6520"> <dc:format>application/pdf</dc:format> <dc:contributor>Butscher, Christine</dc:contributor> <dcterms:bibliographicCitation>First publ. in: Journal of Membrane Biology 168 (1999), pp. 169-181</dcterms:bibliographicCitation> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dcterms:abstract xml:lang="eng">A fluorescence method was adapted to investigate active ion transport in membrane preparations of the SR-Ca-ATPase. The styryl dye RH421 previously used to investigate the Na,K-ATPase was replaced by an analogue, 2BITC, to obtain optimized fluorescence changes upon substrate-induced partial reactions. Assuming changes of the local electric field to be the source of fluorescence changes that are produced by uptake/release or by movement of ions inside the protein, 2BITC allowed the determination of electrogenic partial reactions in the pump cycle. It was found that Ca2+ binding on the cytoplasmic and on the lumenal side of the pump is electrogenic while phosphorylation and conformational transition showed only minor electrogenicity. Ca2+ equilibrium titration experiments at pH 7.2 in the two major conformations of the protein indicated cooperative binding of two Ca2+ ions in state E1 with an apparent half-saturation concentration, KM of 600 nm. In state P-E2 two KM values, 5 μm and 2.2 mM, were determined and are in fair agreement with published data. From Ca2+ titrations in buffers with various pH and from pH titrations in P-E2, it could be demonstrated that H+ binding is electrogenic and that Ca2+ and H+ compete for the same binding site(s). Tharpsigargin-induced inhibition of the Ca-ATPase led to a state with a specific fluorescence level comparable to that of state E1 with unoccupied ion sites, independent of the buffer composition.</dcterms:abstract> <dc:language>eng</dc:language> <dc:creator>Butscher, Christine</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:26:44Z</dcterms:available> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:26:44Z</dc:date> <dcterms:title>Electrogenic partial reactions of the SR-Ca-ATPase investigated by a fluorescence method</dcterms:title> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dcterms:issued>1999</dcterms:issued> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6520"/> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:creator>Roudna, Milena</dc:creator> <dc:contributor>Roudna, Milena</dc:contributor> </rdf:Description> </rdf:RDF>

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