KINETICS OF LYSOZYME REFOLDING FACILITATED BY MOLECULAR CHAPERONE GroEL
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KINETICS OF LYSOZYME REFOLDING FACILITATED BY MOLECULAR CHAPERONE GroEL
CIESC JournalIssue 12, (2001)
作者机构:
天津大学化工学院生物工程系
作者简介:
基金信息:
DOI:
CLC:
Online First:25 December 2001,
Published:25 December 2001
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DONG Xiaoyan, BAI Shu, LIU Xiaoguang, et al. KINETICS OF LYSOZYME REFOLDING FACILITATED BY MOLECULAR CHAPERONE GroEL[J]. CIESC Journal, 2001, (12).
DOI:
DONG Xiaoyan, BAI Shu, LIU Xiaoguang, et al. KINETICS OF LYSOZYME REFOLDING FACILITATED BY MOLECULAR CHAPERONE GroEL[J]. CIESC Journal, 2001, (12).DOI:
KINETICS OF LYSOZYME REFOLDING FACILITATED BY MOLECULAR CHAPERONE GroEL
An apparent kinetic model for lysozyme refolding was established
and the refolding behavior of denatured lysozyme facilitated by the molecular chaperone GroEL was studied.The effects of denatured lysozyme concentration
adenosine triphosphate (ATP) concentration
and the molar ratio of GroEL to lysozyme on the refolding yield and the refolding rate constant were investigated.The lysozyme concentration showed more significant effect on the refolding rate constant than on the refolding yield.Both refolding yield and refolding rate constant increased with increasing ATP concentration.At a definite protein concentration
optimal concentrations of both GroEL and ATP existed to give maximum refolding yield and refolding rate constant.