Study on the binding of cerium to bovine serum albumin

✍ Scribed by Dong Yuan; Zhonglan Shen; Rutao Liu; Zhenxing Chi; Jianhua Zhu

• Publisher: John Wiley and Sons
• Year: 2011
• Tongue: English
• Weight: 120 KB
• Volume: 25
• Category: Article
• ISSN: 1095-6670
• DOI: 10.1002/jbt.20385

✦ Synopsis

Abstract

The interaction of Ce^3+^ to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UV–vis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by Ce^3+^ was a static quenching process, the binding constant is 6.70 × 10^5^, and the number of binding site is 1. The thermodynamic parameters (Δ__H__ = −29.94 kJ mol^−1^, Δ__G__ = −32.38 kJ mol^−1^, and Δ__S__ = 8.05 J mol^−1^ K^−1^) indicate that electrostatic effect between the protein and the Ce^3+^ is the main binding force. In addition, UV–vis, CD, and synchronous fluorescence results showed that the addition of Ce^3+^ changed the conformation of BSA. © 2011 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:263–268, 2011; View this article online at wileyonlinelibrary.com. DOI 10.1002/jbt.20385