An equilibrium and a kinetic stopped-flow fluorescence study of the binding of various metal ions to goat alpha-lactalbumin.

Various metal ions bind to the protein alpha-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.