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Title: Thermodynamics of the Ca2+ binding to bovine alpha-lactalbumin
Authors: Van Ceunebroeck, J C ×
Hanssens, Ignace
Joniau, Marcel
Van Cauwelaert, F #
Issue Date: 15-Aug-1985
Series Title: Journal of Biological Chemistry vol:260 issue:20 pages:10944-7
Abstract: Bovine alpha-lactalbumin contains one strong Ca2+-binding site. The free energy (delta G0), enthalpy (delta H0), and entropy (delta S0) of binding of Ca2+ to this site have been calculated from microcalorimetric experiments. The enthalpy of binding was dependent on the metal-free bovine alpha-lactalbumin concentration. At 0.8 mg ml-1, metal-free bovine alpha-lactalbumin delta H0 was -110 +/- 6 kJ mol-1. At this concentration the binding constant was estimated from a mathematical analysis of the titration curves to be greater than 10(7) M-1. This means that delta G0 is smaller than -40 kJ mol-1 and delta S0 is less negative than -235 J.K-1 mol-1. The binding of Ca2+ is therefore enthalpy-driven. From binding experiments as a function of temperature, a delta Cp value of -4.1 kJ.K-1 mol-1 was calculated. This value is dependent on the protein concentration. A tentative explanation for this large value is given.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Faculty of Science, Campus Kulak Kortrijk
Faculty of Medicine, Campus Kulak Kortrijk
× corresponding author
# (joint) last author

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