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Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase

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MYERS, Sian L., Flemming CORNELIUS, Hans-Jürgen APELL, Ronald J. CLARKE, 2011. Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase. In: Biophysical Journal. 100(1), pp. 70-79. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2010.11.038

@article{Myers2011Kinet-7976, title={Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase}, year={2011}, doi={10.1016/j.bpj.2010.11.038}, number={1}, volume={100}, issn={0006-3495}, journal={Biophysical Journal}, pages={70--79}, author={Myers, Sian L. and Cornelius, Flemming and Apell, Hans-Jürgen and Clarke, Ronald J.} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Myers, Sian L.</dc:contributor> <dcterms:bibliographicCitation>First publ. in: Biophysical Journal 100 (2011), 1, pp. 70-79</dcterms:bibliographicCitation> <dspace:isPartOfCollection rdf:resource=""/> <dspace:hasBitstream rdf:resource=""/> <dcterms:hasPart rdf:resource=""/> <dc:format>application/pdf</dc:format> <dc:date rdf:datatype="">2011-03-24T17:38:59Z</dc:date> <dc:contributor>Clarke, Ronald J.</dc:contributor> <dcterms:abstract xml:lang="eng">Investigations of K+-occlusion by the phosphoenzyme of Na+,K+-ATPase from shark rectal gland and pig kidney by stopped-flow fluorimetry reveal major differences in the kinetics of the two enzymes. In the case of the pig enzyme, a single K+-occlusion step could be resolved with a rate constant of 342 (±26) s−1. However, in the case of the shark enzyme, two consecutive K+-occlusions were detected with rate constants of 391 (±19) s−1 and 48 (±2) s−1 at 24°C and pH 7.4. A conformational change of the phosphoenzyme associated with K+-occlusion is, thus, the major rate-determining step of the shark enzyme under saturating concentrations of all substrates, whereas for the pig enzyme the major rate-determining step under the same conditions is the E2 → E1 transition and its associated K+ deocclusion and release to the cytoplasm. The differences in rate constants of the K+ occlusion reactions of the two enzymes are paralleled by compensating changes to the rate constant for the E2 → E1 transition, which explains why the differences in the enzymes' kinetic behaviors have not previously been identified.</dcterms:abstract> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dc:creator>Myers, Sian L.</dc:creator> <dcterms:available rdf:datatype="">2011-03-24T17:38:59Z</dcterms:available> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Cornelius, Flemming</dc:creator> <dcterms:rights rdf:resource=""/> <dcterms:issued>2011</dcterms:issued> <dc:creator>Clarke, Ronald J.</dc:creator> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dc:language>eng</dc:language> <dcterms:isPartOf rdf:resource=""/> <bibo:uri rdf:resource=""/> <dc:contributor>Cornelius, Flemming</dc:contributor> <dcterms:title>Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase</dcterms:title> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:rights>terms-of-use</dc:rights> </rdf:Description> </rdf:RDF>

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