title: Study on the binding of cerium to bovine serum albumin.
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 (ΔH = -29.94 kJ mol(-1) , ΔG = -32.38 kJ mol(-1) , and ΔS = 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.
authors.affiliation: Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment & Health, Shandong Province, Jinan 250100, People's Republic of China.
authors.forename: Dong
authors.initials: D
authors.lastname: Yuan
authors.forename: Zhonglan
authors.initials: Z
authors.lastname: Shen
authors.forename: Rutao
authors.initials: R
authors.lastname: Liu
authors.forename: Zhenxing
authors.initials: Z
authors.lastname: Chi
authors.forename: Jianhua
authors.initials: J
authors.lastname: Zhu
mesh_terms: D000818:Animals; D002417:Cattle; D002563:Cerium / Q000737:chemistry*; D002942:Circular Dichroism; D006860:Hydrogen Bonding; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine; D002563:Cerium