Article

Development and characterization of an immunoaffinity column for the selective extraction of bisphenol A from serum samples.

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.
Journal of Chromatography B (impact factor: 2.89). 02/2003; 783(2):401-10. pp.401-10
Source: PubMed

ABSTRACT 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.

0 0
 · 
0 Bookmarks
 · 
21 Views
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.

Keywords

affinity
 
binding solvent
 
CNBr-activated Sepharose 4B
 
covalently coupling polyclonal antibodies
 
estrogenic bisphenols
 
immunoaffinity column
 
nonspecific adsorption
 
optimal
 
Proteins
 
serum samples