Kinetic model of lysozyme renaturation with the molecular chaperone GroEL

Biotechnology Letters

Volumn 23, Issue 14, 2001, Pages 1165-1169

  Dong, Xiao Yan ^a   Wang, Yu Bing ^a   Liu, Xiao Guang ^a   Sun, Yan ^a  

^a TIANJIN UNIVERSITY   (China)

Author keywords

GroEL; Kinetics; Lysozyme; Model; Renaturation

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; CHAPERONIN; LYSOZYME;

ARTICLE; ENZYME DENATURATION; ENZYME KINETICS; ENZYME MECHANISM; MODEL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN RENATURATION;

EID: 0034859904     PISSN: 01415492     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010504824604     Document Type: Article

References (13)

1. Lysozyme reactivation using immobilized molecular chaperonin GroEL
2. Lysozyme refolding with immobilized GroEL column chromatography
3. Molecular chaperones
4. Promotion of the in vitro renaturation of dodecametric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP
5. Recovery and reuse of the molecular chaperone GroEL for in vitro protein refolding
6. Oxidative renaturation of lysozyme at high concentrations
7. DNA fragment containing the groE genes can suppress mutations in Escherichia coli dnaA genes
8. Bacterial chaperones increase the production of soluble human TNF-α Escherichia coli
9. Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme
10. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanase
11. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: Modulation of the competition between renaturation and aggregation
12. Reactivation of thermally inactivated enzymes by free and immobilized chaperonin GroEL/ES
13. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL