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How phospholamban could affect the apparent affinity of Ca 2+ ‐ATPase for Ca 2+ in kinetic experiments
Author(s) -
Lee Anthony G
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00869-x
Subject(s) - phospholamban , endoplasmic reticulum , calcium atpase , atpase , chemistry , kinetic energy , biophysics , binding site , calcium , kinetic scheme , enzyme , crystallography , biochemistry , biology , physics , organic chemistry , quantum mechanics
Binding of phospholamban (PLN) to the Ca 2+ ‐ATPase of muscle sarcoplasmic reticulum results in a decrease in apparent affinity for Ca 2+ without affecting the true binding constant for Ca 2+ 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 Ca 2+ ‐ATPase.