An Equilibrium and a Kinetic Stopped-Flow Fluorescence Study of the Binding of Various Metal Ions to Goat Alpha-Lactalbumin

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Abstract

Various metal ions bind to the protein α-lactalbumin prepared from goat milk. The stability of the protein after metal binding is compared with that of the apo-protein by monitoring the fluorescence of the tryptophan residues under equilibrium conditions. The kinetics of the metal binding is studied by stopped-flow fluorescence spectroscopy. By means of the Arrhenius plots, the activation energy with regard to the binding of the different ions is determined.

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