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An experimental artifact in the use of chelating metal ion buffers. Binding of chelators to bovine alpha-lactalbumin
Journal of Biological Chemistry
The binding of EDTA and EGTA to bovine alpha-lactalbumin was shown to stabilize the native conformation relative to that characteristic of the metal-free protein (A conformer). Fluorescence titration of the metal-free protein with Ca2+ in the presence of EDTA was markedly influenced by micromolar concentrations of EDTA such that the apparent association constant of calcium binding would be significantly larger than obtained in the absence of chelator. These observations explain the discrepancypmid:6406505 fatcat:udvshuvtmjcfjgapkicbqotqo4