Article citationsMore>>
Y. J. Shiu, U. S. Jeng, Y. S. Huang, Y. H. Lai, H. F. Lu, C. T. Liang, I. J. Hsu, C. H. Su, C. Su, I. Chao, A. C. Su and S. H. Lin, “Global and Local Structural Changes of Cytochrome C and Lysozyme Characterized by a Multigroup Unfolding Process,” Biophysical Journal, Vol. 94, No. 12, 2008, pp. 4828-4836.
doi:10.1529/biophysj.107.124214
has been cited by the following article:
-
TITLE:
Pressure- and Urea-Induced Denaturation of Bovine Serum Albumin: Considerations about Protein Heterogeneity
AUTHORS:
Douglas Ricardo Norberto, Joelma Mauricio Vieira, Ancelmo Rabelo de Souza, Jose Ailton Conceicao Bispo, Carlos Francisco Sampaio Bonafe
KEYWORDS:
Apparent Stoichiometric Coefficient; Bovine Serum Albumin; High Pressure-Induced Denaturation; Protein Heterogeneity; Urea-Induced Denaturation
JOURNAL NAME:
Open Journal of Biophysics,
Vol.2 No.1,
January
19,
2012
ABSTRACT: Urea denatures proteins at different concentrations, depending on the experimental conditions and the protein. We in-vestigated the pressure-induced denaturation of bovine serum albumin (BSA) in the presence of subdenaturing concen-trations of urea based on a two-state equilibrium. Pressure-induced denaturation was enhanced at urea concentrations ([U]) of 3.5 M to 8.0 M, with the free energy of denaturation at atmospheric pressure ranging from +5.0 to –2.5 kJ/mol of BSA. The m values appeared to be biphasic, with m1 and m2 of 0.92 and 2.35 kJ mol–1?M–1, respectively. Plots of versus ln[U] yielded values of u, the apparent stoichiometric coefficient, of 1.68 and 6.67 mol of urea/mol of BSA for m1 and m2, respectively. These values were compared with the m and u values of other monomeric proteins reported in or calculated from the literature. The very low values of u systematically observed for proteins were suggestive of heterogeneity in the free energy of denaturation. Thus, a u value of 140 mol of urea/mol of BSA may indicate the existence of a heterogeneous molecular population with respect to the free energy of dena-turation.