Document Detail

Biochemical characterization of human peroxiredoxin 2, an antioxidative protein.
MedLine Citation:
PMID:  22805285     Owner:  NLM     Status:  Publisher    
Human peroxiredoxin 2 (Prx2), which is abundant in erythrocytes, has been shown to play a key role in protecting erythrocytes against oxidative stress by scavenging reactive oxygen species as well as participating in cell signal transduction. Here, human Prx2 gene was successfully cloned into Escherichia coli BL21 (DE3) for Prx2 expression. Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis suggested that the recombinant protein was expressed mainly in a soluble form. The recombinant protein was purified by one-step Ni-nitrilotriacetic acid chelating affinity chromatography to a purity of up to 91.5%. The peroxidase activity of Prx2 to scavenge H(2)O(2) was determined by a ferrithiocyanate assay. The ability of Prx2 to protect plasmid DNA was tested by using a mixed-function oxidation system, and results showed that Prx2 could prevent DNA from undergoing oxidative stress. Ultraviolet (UV)-induced cell apoptosis assay demonstrated that Prx2 is also able to protect NIH/3T3 cells from UV-induced damage, suggesting its possible applications in cosmetics and other areas.
Sheng Yan; Shaopei Chen; Zhendong Li; Haiying Wang; Tuxiong Huang; Xiaoning Wang; Jufang Wang
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-17
Journal Detail:
Title:  Acta biochimica et biophysica Sinica     Volume:  -     ISSN:  1745-7270     ISO Abbreviation:  -     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-7-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101206716     Medline TA:  Acta Biochim Biophys Sin (Shanghai)     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China.
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