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  • Title: Lipid requirement of the vanadate effect on the binding of calcium and ATP to the calcium transport ATPase of the sarcoplasmic reticulum.
    Author: Medda P, Hasselbach W.
    Journal: Eur J Biochem; 1985 Jan 15; 146(2):255-60. PubMed ID: 3155683.
    Abstract:
    Lipid deprivation of the sarcoplasmic reticulum calcium-transport ATPase neither affects the enzyme's affinity for ATP nor that of calcium. In contrast, vanadate binding is almost completely abolished. Lipid substitution by oleic acid which at a ratio of 0.3 mg/mg protein completely reactivates the calcium-dependent ATP hydrolysis restores vanadate binding. Concomitantly the mutual interactions between vanadate and calcium or ATP and ADP, respectively are restored. The vanadate-induced disappearance of the enzyme's ATP binding sites as well as its high-affinity binding sites for calcium follow the same time course. Conversely, the displacement of vanadate by calcium proceeds in parallel with the recovery of ADP binding. In lipid-restituted preparations as well as in native membranes vanadate induces the disappearance of external high-affinity and simultaneously the appearance of internal low-affinity calcium binding sites.
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