title: Use of zeolite to refold a disulfide-bonded protein.
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.
authors.affiliation: Research Center for Compact Chemical Process, AIST, Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan.
authors.forename: Takayuki Y
authors.initials: TY
authors.lastname: Nara
authors.forename: Hideaki
authors.initials: H
authors.lastname: Togashi
authors.forename: Chisato
authors.initials: C
authors.lastname: Sekikawa
authors.forename: Masayuki
authors.initials: M
authors.lastname: Kawakami
authors.forename: Nakatsugu
authors.initials: N
authors.lastname: Yaginuma
authors.forename: Kengo
authors.initials: K
authors.lastname: Sakaguchi
authors.forename: Fujio
authors.initials: F
authors.lastname: Mizukami
authors.forename: Tatsuo
authors.initials: T
authors.lastname: Tsunoda
mesh_terms: D004220:Disulfides / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D010084:Oxidation-Reduction; D017510:Protein Folding; D017641:Zeolites / Q000737:chemistry*
chemical_list: D004220:Disulfides; D017641:Zeolites; C421864:hen egg lysozyme; D009113:Muramidase