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Studies on the Refolding of Egg White Lysozyme Denatured by Urea Using "Phase Diagram" Method of Fluorescence
Author(s) -
BIAN LiuJiao,
DONG FaXin,
LIANG ChangLi,
YANG XiaoYan,
LIU Li
Publication year - 2007
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200790350
Subject(s) - lysozyme , chemistry , urea , egg white , chromatography , phase diagram , phase (matter) , biochemistry , organic chemistry
The refolding of reduced and non‐reducing egg white lysozymes in a urea solution was studied by a "phase diagram" method of fluorescence. The result showed that in the refolding of the reduced egg white lysozyme, an intermediate state of an egg white lysozyme exists at the urea concentrations in a final renaturation solution being about 4.5 mol/L, their refolding follows a three‐state model; while in the refolding of the non‐reducing egg white lysozyme, two intermediate states exist at the urea concentrations being separately 4.0 and 2.5 mol/L, and their refolding follows a four‐state model. Through the comparison between the unfolding and refolding of an egg white lysozyme in the urea solution, it was found that both of the refolding of reduced and non‐reducing egg white lysozyme molecules was irreversible to their unfolding in the urea solution. Finally, a suggested refolding was separately presented for the reduced and non‐reducing egg white lysozymes in the urea solution.