Refolding of superoxide dismutase by ion-exchange chromatography

Biotechnology Letters

Volumn 24, Issue 11, 2002, Pages 919-923

  Li, Ming ^a   Su, Zhi Guo ^a  

^a INSTITUTE OF PROCESS ENGINEERING   (China)

Author keywords

Gradient ion exchange chromatography; Inclusion body; pH; Refolding; Superoxide dismutase; Urea concentration

Indexed keywords

BUFFER; IRON SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; UREA;

ADSORPTION; ARTICLE; ENZYME ACTIVITY; ESCHERICHIA COLI; ION EXCHANGE CHROMATOGRAPHY; NONHUMAN; PH; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036276966     PISSN: 01415492     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1015596211026     Document Type: Article

References (10)

1. Principles that govern the folding of protein chains
2. Refolding of recombinant proteins
3. Protein refolding for industrial processes
4. Impact of protein folding on biotechnology
5. Urea gradient size-exclusion chromatography enhanced the yield of lysozyme refolding
6. Oxidative renaturation of lysozyme at high concentrations
7. High yield refolding of lysozyme and carbonic anhydrase at high protein concentration
8. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
9. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies
10. High-level expression of Mycoplasma arginine deiminase in Esherichia coli and its efficient renaturation as an anti-tumor enzyme