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A spectroscopic approach of pH effect on thermal denaturation of human and bovine serum albumins

C. G. CHILOM1,* , G. BARANGĂ1, D. M. GĂZDARU1, A. POPESCU1

Affiliation

  1. Faculty of Physics, University of Bucharest, Bucharest, Romania

Abstract

Thermal conformational changes of human serum albumin (HSA) and bovine serum albumin (BSA) in different buffer solutions, in the pH range 3.0 - 9.0, are investigated by fluorescence spectroscopy. Temperature increasing in the range 25 - 90 oC induces partially reversible changes in the 3D structure of the two serum albumins. At pH = 3.0 (albumin form E) and pH = 8.0 (B form) the renaturation degree is greater than that manifested at pH = 4.0 (F form) and pH = 7.0 (N form). Instead, at pH = 5.0 and pH = 6.0, both serum albumins present states, whose thermal denatured conformations cannot be renatured by a stepwise temperature decrease..

Keywords

Albumins, Trp fluorescence, pH, Thermal denaturation/renaturation.

Submitted at: Feb. 3, 2011
Accepted at: May 25, 2011

Citation

C. G. CHILOM, G. BARANGĂ, D. M. GĂZDARU, A. POPESCU, A spectroscopic approach of pH effect on thermal denaturation of human and bovine serum albumins, Journal of Optoelectronics and Advanced Materials Vol. 13, Iss. 5, pp. 583-587 (2011)