Development and characterization of an immunoaffinity column for the selective extraction of bisphenol A from serum samples.
An immunoaffinity column (IAC) was developed by covalently coupling polyclonal antibodies against estrogenic bisphenols to CNBr-activated Sepharose 4B. The IAC showed high affinity for bisphenol A, while phenol was barely retained. Proteins in the sample matrix showed little nonspecific adsorption on the column. The best binding solvent for bisphenol A was found to be 0.01 mol l(-1) phosphate-buffered saline (PBS) and the optimal operating temperature was 4 degrees C. The bound bisphenol A could be quantitatively recovered by 1 ml of methanol-water (80:20) with an average recovery of 91.8% and a relative standard deviation of 7.1% (n=6). The immunoaffinity column has been successfully used for the isolation and purification of bisphenol A from serum samples.
Zhao
Meiping
M
The Key Laboratory of Bioorganic Chemistry and Molecular Engineering, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, 100871, Beijing, PR China. mpzhao@chem.pku.edu.cn
Liu
Yang
Y
Li
Yuanzong
Y
Zhang
Xinxiang
X
Chang
Wenbao
W
D000818:Animals; D001559:Benzhydryl Compounds; D002846:Chromatography, Affinity / Q000295:instrumentation*; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D051379:Mice; D008807:Mice, Inbred BALB C; D010636:Phenols / Q000097:blood*; D013056:Spectrophotometry, Ultraviolet; D000098826:Bisphenol A Compounds
D001559:Benzhydryl Compounds; D010636:Phenols; C006780:bisphenol A; D000098826:Bisphenol A Compounds