Abstract: An Nterminal 32 amino acids radish PHGPx gene (Δ32RsPHGPx) was cloned into expression vector pGEX-6P-1 and transformed into E.coli strain BL21 (DE3). Δ32RsPHGPx for crystallization was prepared via Glutathione SepharoseTM affinity, cationexchange and gel filtration chromatographies. Theconcentration of it was 10 g/L and the purity was over 95%. Δ32RsPHGPx showed obvious PHGPx activity towardslipid hydroperoxides. In addition, a tertiary structure model of Δ32RsPHGPx displayed the thioredoxin fold.

Key words: radish, phospholipid hydroperoxide glutathione peroxidase, expression, purification