Abstract
Near-UV circular dichroism and differential scanning calorimetry were used to analyse the thermal denaturation of bovine α-lactalbumin at pH 7.5 and various Ca2+ concentrations. Both analyses revealed that the denaturated protein consists of two fractions, a Ca2+-loaded and a Ca2+-free fraction. Despite this agreement, the two methods afforded significantly different values for the thermodynamic parameters of the denaturations. It was demonstrated that the ellipticity changes were more appropriate than the excess heat capacities for analysis of the two types of denaturation. The values of the thermodynamic parameters obtained with the former method are therefore more reliable.
Similar content being viewed by others
References
K. R. Acharya, D. I. Stuart, N. R C. Walker, M. Lewis and D. C. Philips, J. Mol. Biol., 208 (1989) 99.
H. A. McKenzie and F. H. White, Adv. Protein Chem., 41 (1991) 173.
J. Desmet and F. Van Cauwelaert, Biochim. Biophys. Acta, 912 (1988) 211.
P. Relkin, Crit. Rev. Food Sci. Nutr., 36 (1996) 565.
P. Haezebrouck, A. De Baetselier, M. Joniau, H. Van Dael, S. Rosenberg and I. Hanssens, Protein Eng., 6 (1993) 643.
R. Kuroki, K. Nitta and K. Yutani, J. Biol. Chem., 267 (1992) 24297.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Hanssens, I., Vanderheeren, G. Thermodynamic Characterization of Two Nearly Simultaneous Protein Denaturations. Journal of Thermal Analysis 51, 871–877 (1998). https://doi.org/10.1007/BF03341464
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF03341464