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