albumin - publications

Predict more albumin - ligand interactions now!

1. J Chromatogr A. 2012 May 3. [Epub ahead of print]

Enhancing IgG purification from serum albumin containing feedstock with
hydrophobic charge-induction chromatography.

Tong HF, Lin DQ, Yuan XM, Yao SJ.

State Key Laboratory of Chemical Engineering, Department of Chemical and
Biological Engineering, Zhejiang University, Hangzhou 310027, China.

Hydrophobic charge-induction chromatography (HCIC) with 4-mercaptoethyl-pyridine
(MEP) as the ligand is a novel technology for antibody purification, however, the
separation selectivity still needs to be improved for the applications,
especially for the impurity of serum albumin. In this study, with bovine serum
immunoglobulin G (IgG) as the model, the purification of IgG from the serum
albumin containing feedstock was developed with the commercial HCIC resin MEP
HyperCel, focusing on the optimization of operation pH and salt addition. The
adsorption isotherms of IgG and bovine serum albumin (BSA) were investigated at
different pHs, and the binding and elution behaviors of two proteins in the
column were also studied at varying pHs. In addition, the protein-ligand
interactions were investigated with some additives in the buffer. It was found
that the conditions of pH 6 with 0.1M NaCl or pH 8 could be used to effectively
remove BSA from the MEP resin without the influence on IgG adsorption. Two modes
with control of loading or washing buffer were tested to enhance the purification
of IgG from BSA containing feedstock, and the purity of IgG was improved to about
95% compared with 62.9% for the control. The results demonstrated that the
control of loading pH or the addition of NaCl in the buffer might be an effective
method to improve the purification of antibody with the HCIC process.

Copyright © 2012 Elsevier B.V. All rights reserved.

PMID: 22609164 [PubMed - as supplied by publisher]