Properties of the SR Ca-ATPase in an Open Microsomal Membrane Preparation

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FIBICH, Andreas, Christian JÜNGST, Hans-Jürgen APELL, 2008. Properties of the SR Ca-ATPase in an Open Microsomal Membrane Preparation. In: The Open Biochemistry Journal. 2, pp. 91-99. ISSN 1874-091X. eISSN 1874-091X

@article{Fibich2008Prope-6908, title={Properties of the SR Ca-ATPase in an Open Microsomal Membrane Preparation}, year={2008}, doi={10.2174/1874091X00802010091}, volume={2}, issn={1874-091X}, journal={The Open Biochemistry Journal}, pages={91--99}, author={Fibich, Andreas and Jüngst, Christian 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/123456789/6908"> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dc:contributor>Jüngst, Christian</dc:contributor> <dc:contributor>Fibich, Andreas</dc:contributor> <dc:creator>Jüngst, Christian</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6908"/> <dcterms:abstract xml:lang="eng">SR vesicles isolated from rabbit muscle were treated by a SDS incubation and subsequent dialysis to obtain open membrane fragments that allow a direct access to the luminal membrane surface and especially to the ion-binding sites in the P-E2 conformation of the Ca-ATPase. The open membrane fragments showed about 80% of the enzyme activity in the untreated membranes. Pump function was investigated by using electrochromic styryl dyes. The kinetic properties of cytoplasmic ion binding showed no significant differences between the Ca-ATPases in SR vesicles and in membrane fragments. From pH-dependent Ca2+ binding it could be deduced that due to the SDS treatment the density of negatively charged lipid was increased by one elementary charge per 12 lipid molecules. Major differences between Ca-ATPase from SR vesicles and membrane fragments were the respective fluorescence amplitudes. This effect is, however, produced by dye-lipid interaction and not by pump function. It was demonstrated that time-resolved kinetics may be study by the use of caged compounds such as caged ATP or caged calcium also in the case of the membrane fragments.</dcterms:abstract> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dcterms:title>Properties of the SR Ca-ATPase in an Open Microsomal Membrane Preparation</dcterms:title> <dc:format>application/pdf</dc:format> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:04Z</dc:date> <dcterms:issued>2008</dcterms:issued> <dc:language>eng</dc:language> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:creator>Fibich, Andreas</dc:creator> <dc:rights>deposit-license</dc:rights> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:04Z</dcterms:available> <dcterms:bibliographicCitation>First publ. in: The Open Biochemistry Journal 2 (2008), pp. 91-99</dcterms:bibliographicCitation> </rdf:Description> </rdf:RDF>

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