Use of zeolite to refold a disulfide-bonded protein
| Autor: | Chisato Sekikawa, Fujio Mizukami, Masayuki Kawakami, Takayuki Y. Nara, Hideaki Togashi, Tatsuo Tsunoda, Nakatsugu Yaginuma, Kengo Sakaguchi |
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| Rok vydání: | 2009 |
| Předmět: |
Protein Folding
Surfaces and Interfaces General Medicine Polyethylene glycol Microporous material chemistry.chemical_compound Colloid and Surface Chemistry Adsorption chemistry Aluminosilicate Reagent Polymer chemistry Zeolites Organic chemistry Muramidase Disulfides Physical and Theoretical Chemistry Lysozyme Guanidine Zeolite Oxidation-Reduction Biotechnology |
| Zdroj: | Colloids and Surfaces B: Biointerfaces. 68:68-73 |
| ISSN: | 0927-7765 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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