Recombinant human peroxiredoxin VI: preparation and protective properties in vitro

cDNA of human peroxiredoxin VI, one of the recently discovered novel antioxidant proteins, was expressed in Escherichia coli cells. The expression product was obtained in water-soluble form and purified by a two-step chromatographic procedure using DEAE-Sepharose and Sephacryl S-200. According to CD...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2002-11, Vol.67 (11), p.1235-1239
Main Authors: Merkulova, M I, Shuvaeva, T M, Radchenko, V V, Yanin, B A, Bondar, A A, Sofin, A D, Lipkin, V M
Format: Article
Language:English
Subjects:
Animals
Antioxidants - isolation & purification
Antioxidants - pharmacology
Bacteria
Chromatography, Ion Exchange - methods
Circular Dichroism
Cloning, Molecular
DNA, Complementary - biosynthesis
E coli
Enzymes
Escherichia coli - enzymology
Escherichia coli - genetics
Genetic Vectors - genetics
Glutamate-Ammonia Ligase - drug effects
Glutamate-Ammonia Ligase - metabolism
Humans
Inactivation
Oxidation-Reduction
Peroxidases - biosynthesis
Peroxidases - genetics
Peroxidases - isolation & purification
Peroxidases - pharmacology
Peroxiredoxin VI
Peroxiredoxins
Protein Structure, Secondary
Rats
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Recombinant Proteins - pharmacology
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Summary:cDNA of human peroxiredoxin VI, one of the recently discovered novel antioxidant proteins, was expressed in Escherichia coli cells. The expression product was obtained in water-soluble form and purified by a two-step chromatographic procedure using DEAE-Sepharose and Sephacryl S-200. According to CD data, the polypeptide chain of the recombinant human peroxiredoxin VI contains approximately 40% alpha-helical region and 30% beta-structure, which is the same as for native rat peroxiredoxin VI. The protective properties of the recombinant protein determined as its ability to prevent the inactivation of glutamine synthetase from E. coli in a model oxidation system were comparable with the protective properties of native rat peroxiredoxin VI.
ISSN:0006-2979
1608-3040
DOI:10.1023/A:1021345203977