Recombinant Human Peroxiredoxin VI: Preparation and Protective Properties in vitro

M. I. Merkulova^1*, T. M. Shuvaeva¹, V. V. Radchenko¹, B. A. Yanin², A. A. Bondar², A. D. Sofin², and V. M. Lipkin¹

¹Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 177997 Russia; fax: (095) 335-7103; E-mail: mmer@mail.ibch.ru

²Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia; fax: (096) 779-0509; E-mail: novoselov@mail.icb.psn.ru

^* To whom correspondence should be addressed.

Received April 30, 2002

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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 ~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.

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KEY WORDS: reactive oxygen species, antioxidant, peroxiredoxin VI

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