How phospholamban could affect the apparent affinity of Ca2+-ATPase for Ca2+ in kinetic experiments
How phospholamban could affect the apparent affinity of Ca2+-ATPase for Ca2+ in kinetic experiments
Binding of phospholamban (PLN) to the Ca2+-ATPase of muscle sarcoplasmic reticulum results in a decrease in apparent affinity for Ca2+ without affecting the true binding constant for Ca2+ determined in equilibrium binding experiments. It is shown that this can be explained by a scheme in which the ATPase shows two modes of binding for PLN, one of high and one of low affinity; the proposed scheme is not dependent on the kinetic model assumed for the Ca2+-ATPase.
phospholamban, Ca2+-ATPase, calcium binding, sarcoplasmic reticulum, kinetic simulation
37-41
Lee, Anthony G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
11 September 2003
Lee, Anthony G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Lee, Anthony G.
(2003)
How phospholamban could affect the apparent affinity of Ca2+-ATPase for Ca2+ in kinetic experiments.
FEBS Letters, 551 (1), .
(doi:10.1016/S0014-5793(03)00869-X).
Abstract
Binding of phospholamban (PLN) to the Ca2+-ATPase of muscle sarcoplasmic reticulum results in a decrease in apparent affinity for Ca2+ without affecting the true binding constant for Ca2+ determined in equilibrium binding experiments. It is shown that this can be explained by a scheme in which the ATPase shows two modes of binding for PLN, one of high and one of low affinity; the proposed scheme is not dependent on the kinetic model assumed for the Ca2+-ATPase.
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Submitted date: 27 May 2003
Published date: 11 September 2003
Keywords:
phospholamban, Ca2+-ATPase, calcium binding, sarcoplasmic reticulum, kinetic simulation
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Local EPrints ID: 56533
URI: http://eprints.soton.ac.uk/id/eprint/56533
ISSN: 0014-5793
PURE UUID: ed65df83-7bc7-40a7-927d-227ff64441c6
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Date deposited: 07 Aug 2008
Last modified: 15 Mar 2024 11:02
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