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.
Van Dael
H
H
Interdisciplinary Research Centre, K.U. Leuven Campus Kortrijk, Sabbelaan 53, 8500 Kortrijk, Belgium. herman.vandael@kuleuven-kortrijk.be
Chedad
A
A
D000818:Animals; D005453:Fluorescence; D006041:Goats; D006358:Hot Temperature; D007700:Kinetics; D007768:Lactalbumin / Q000737:chemistry / Q000378:metabolism*; D008670:Metals / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D008670:Metals; D007768:Lactalbumin