Use of zeolite to refold a disulfide-bonded protein
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- 作者：Takayuki Y. Nara ; Hideaki Togashi ; Chisato Sekikawa ; Masayuki Kawakami ; Nakatsugu Yaginuma ; Kengo Sakaguchi ; Fujio Mizukami ; Tatsuo Tsunoda
- 关键词：Zeolite ; Refolding ; Disulfide bond ; Redox ; Lysozyme
- 刊名：Colloids and Surfaces B: Biointerfaces
- 出版年：2009
- 出版时间：1 January 2009
- 年：2009
- 卷：68
- 期：1
- 页码：68-73
- 全文大小：182 K
文摘
Zeolites are microporous crystalline aluminosilicates with a highly ordered structure. Using zeolite beta as an adsorbent, denatured/reduced hen egg lysozyme was refolded to the active form at high concentrations. The denatured/reduced lysozyme was adsorbed onto the zeolite and the protein was refolded by desorbing it into refolding buffer, consisting of redox reagents, guanidine hydrochloride, polyethylene glycol, and l-arginine. This zeolite refolding method could be highly effective for various kinds of proteins, refolding them with high efficiency even when they contain disulfide bonds.