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  • Title: Arsenate-induced fluorescence changes in the Ca(2+)-ATPase of sarcoplasmic reticulum membranes.
    Author: Alves EW.
    Journal: Arch Biochem Biophys; 1992 Feb 01; 292(2):613-6. PubMed ID: 1731624.
    Abstract:
    Arsenate, an analogue of inorganic phosphate, causes an increase in the intrinsic fluorescence of the Ca(2+)-ATPase of sarcoplasmic reticulum membranes. This increase in fluorescence is observed regardless of whether Ca(2+)-loaded or leaky vesicles are assayed. The maximal fluorescence change (2-3%) is observed at pH 6.0 in the presence of Mg2+ and is abolished by the addition of micromolar Ca2+ concentrations. Dimethyl sulfoxide (20% v/v) increases the enzyme's affinity for arsenate one order of magnitude. It is concluded that arsenate, after binding, promotes the same conformational change of the enzyme as that produced by Pi.
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