Expression and purification of recombinant human cytochrome C in Escherichia coli / 生物医学工程学杂志
Journal of Biomedical Engineering
;
(6): 620-625, 2007.
Article
in Chinese
| WPRIM
| ID: wpr-357638
ABSTRACT
Cytochrome C plays important roles in electron transferring, oxidative stress and apoptosis. In this study, soluble cytochrome C was accumulated in cytoplasm of E. coli by utilizing the co-expression of human cytochrome c and yeast heme lyase from a single plasmid. After ultrasonic disruption of the bacteria, a lot of contaminated proteins were discarded by addition of 350 g/L ammonium sulfate into the supernatant. Then the recombinant human cytochrome C was purified to 80% homogeneity after two times cation exchange chromatography on SP-Sepharose Fast Flow. Yields of cytochrome C greater than 10 mg per liter culture were attained. This efficient system for producing human cytochrome C is helpful for us to understand the roles of this protein in biological processes and therapy of human diseases relevant to apoptosis and oxidative stress.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Recombinant Proteins
/
Cytochromes c
/
Escherichia coli
/
Genetic Vectors
/
Genetics
/
Metabolism
Limits:
Humans
Language:
Chinese
Journal:
Journal of Biomedical Engineering
Year:
2007
Type:
Article
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