How phospholamban could affect the apparent affinity of Ca2+‐ATPase for Ca2+ in kinetic experiments

FEBS Letters

Lee, Anthony G¹ 

[1] Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK

关键词: Phospholamban;    Ca2+-ATPase;    Calcium binding;    Sarcoplasmic reticulum;    Kinetic simulation;    PLN;    phospholamban;    PLN(25–52);    the transmembrane domain of PLN;    PLNCys−;    PLN with the three Cys residues replaced by Ala;   

DOI  :  10.1016/S0014-5793(03)00869-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown