Aspartic acid incorporated monolithic columns for affinity glycoprotein purification
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- 作者：Canan Armutcu ; Nilay Bereli ; Engin Bayram ; Lokman Uzun ; R谋dvan Say ; Adil Denizli
- 关键词：Monolithic columns ; IgG separation ; Pseudospecific ligands ; High performance liquid chromatography
- 刊名：Colloids and Surfaces B: Biointerfaces
- 出版年：1 February, 2014
- 年：2014
- 卷：114
- 期：Complete
- 页码：67-74
- 全文大小：3763 K
文摘
Novel aspartic acid incorporated monolithic columns were prepared to efficiently affinity purify immunoglobulin G (IgG) from human plasma. The monolithic columns were synthesised in a stainless steel HPLC column (20 cm 脳 5 mm id) by in situ bulk polymerisation of N-methacryloyl-l-aspartic acid (MAAsp), a polymerisable derivative of l-aspartic acid, and 2-hydroxyethyl methacrylate (HEMA). Monolithic columns [poly(2-hydroxyethyl methacrylate-N-methacryloyl-l-aspartic acid) (PHEMAsp)] were characterised by swelling studies, Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The monolithic columns were used for IgG adsorption/desorption from aqueous solutions and human plasma. The IgG adsorption depended on the buffer type, and the maximum IgG adsorption from aqueous solution in phosphate buffer was 0.085 mg/g at pH 6.0. The monolithic columns allowed for one-step IgG purification with a negligible capacity decrease after ten adsorption-desorption cycles.