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Kinetic Investigations of the Mechanism of the Rate-Determing Step of the Na+, K+ -ATPase Pump Cycle

Kinetic Investigations of the Mechanism of the Rate-Determing Step of the Na+, K+ -ATPase Pump Cycle

Type of Publication: Journal article
URI (citable link): http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-39373
Author: Clarke, Ronald J.; Humphrey, Paul; Lüpfert, Christian; Apell, Hans-Jürgen; Cornelius, Flemming
Year of publication: 2003
Published in: Annals of the New York Academy of Science ; 986 (2003), 1. - pp. 159-162. - ISSN 0077-8923. - eISSN 1749-6632
DOI (citable link): https://dx.doi.org/10.1111/j.1749-6632.2003.tb07154.x
Summary:
The kinetics of the E2->E1 conformational change of unphosphorylated Na+ ,K+ -ATPase from rabbit kidney were investigated via the stopped-flow technique using the fluorescent label RH421 (pH 7.4, 24°C). The enzyme was preequilibrated in a solution containing 25 mM histidine and 0.1 mM EDTA to initially stabilize the E2 conformation. On mixing enzyme with NaCl alone, tris-ATP alone, or NaCl and tris-ATP simultaneously, a fluorescence decrease was observed.
Subject (DDC): 570 Biosciences, Biology
Keywords: stopped-flow, fluorescence, voltage-sensitive dye, rate constant, regulation
Link to License: Terms of use
Bibliography of Konstanz: Yes

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CLARKE, Ronald J., Paul HUMPHREY, Christian LÜPFERT, Hans-Jürgen APELL, Flemming CORNELIUS, 2003. Kinetic Investigations of the Mechanism of the Rate-Determing Step of the Na+, K+ -ATPase Pump Cycle. In: Annals of the New York Academy of Science. 986(1), pp. 159-162. ISSN 0077-8923. eISSN 1749-6632. Available under: doi: 10.1111/j.1749-6632.2003.tb07154.x

@article{Clarke2003Kinet-7310, title={Kinetic Investigations of the Mechanism of the Rate-Determing Step of the Na+, K+ -ATPase Pump Cycle}, year={2003}, doi={10.1111/j.1749-6632.2003.tb07154.x}, number={1}, volume={986}, issn={0077-8923}, journal={Annals of the New York Academy of Science}, pages={159--162}, author={Clarke, Ronald J. and Humphrey, Paul and Lüpfert, Christian and Apell, Hans-Jürgen and Cornelius, Flemming} }

Apell, Hans-Jürgen Lüpfert, Christian eng Cornelius, Flemming Clarke, Ronald J. Clarke, Ronald J. application/pdf The kinetics of the E2->E1 conformational change of unphosphorylated Na+ ,K+ -ATPase from rabbit kidney were investigated via the stopped-flow technique using the fluorescent label RH421 (pH 7.4, 24°C). The enzyme was preequilibrated in a solution containing 25 mM histidine and 0.1 mM EDTA to initially stabilize the E2 conformation. On mixing enzyme with NaCl alone, tris-ATP alone, or NaCl and tris-ATP simultaneously, a fluorescence decrease was observed. terms-of-use First publ. in: Annals of the New York Academy of Science 986 (2003), pp. 159-162 Kinetic Investigations of the Mechanism of the Rate-Determing Step of the Na+, K+ -ATPase Pump Cycle Lüpfert, Christian Apell, Hans-Jürgen Cornelius, Flemming Humphrey, Paul 2003 Humphrey, Paul 2011-03-24T17:33:26Z 2011-03-24T17:33:26Z

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