Abstract: Toona sinensis seeds protein (TSP)was extracted by salting out,alkali extraction and acid precipitation,direct heating methods.The total antioxidant and DPPH free radicals scavenge activity of the extract were then evaluated.TSP from alkali extraction and acid precipitation was selected as purification sampleand was purificated by affinity chromatography.Sephadex G-25 were activated using epichlorohydrin,hemin was bound with them to prepare an immobilized hemin affinity chromatography column,which was used to purifyproteins from T.sinensis seeds equilibrated with water and eluted with NaAc-HAc buffer.Purification protein was tested by DPPH free radicals scavenge assay.The results showed that protein content was from 59.51% to 96.23% after affinity chromatography purification.

Key words: Toona sinensis seeds, affinity chromatography, protein purification, antioxidant activity