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  • Title: Direct fluorescence measurements of Mg2+ binding to sarcoplasmic reticulum ATPase.
    Author: Guillain F, Gingold MP, Champeil P.
    Journal: J Biol Chem; 1982 Jul 10; 257(13):7366-71. PubMed ID: 6211442.
    Abstract:
    In the absence of calcium, interaction of magnesium with SR-ATPase induced a blue shift in intrinsic fluorescence emission. This Mg2+-induced fluorescence change was pH-dependent and an apparent Mg dissociation constant of 5 mM was found at pH 7. Equilibrium studies showed that magnesium competes for the high affinity Ca2+ binding sites and stopped flow measurements of the transient kinetics indicated a multistep interaction between magnesium and the calcium pump. These results suggest that magnesium drives the sarcoplasmic reticulum atpase toward an E.Mg species which might be a dead-end complex.
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