Title of article
Use of zeolite to refold a disulfide-bonded protein
Author/Authors
Nara، نويسنده , , Takayuki Y. and Togashi، نويسنده , , Hideaki and Sekikawa، نويسنده , , Chisato and Kawakami، نويسنده , , Masayuki and Yaginuma، نويسنده , , Nakatsugu and Sakaguchi، نويسنده , , Kengo and Mizukami، نويسنده , , Fujio and Tsunoda، نويسنده , , Tatsuo، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2009
Pages
6
From page
68
To page
73
Abstract
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.
Keywords
Lysozyme , redox , disulfide bond , Zeolite , refolding
Journal title
Colloids and Surfaces B Biointerfaces
Serial Year
2009
Journal title
Colloids and Surfaces B Biointerfaces
Record number
1969661
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