Recombinant human IFN-α2 was purified from E. coli by methods involving sonication, extraction with 8 M Guanidine-HCI, dilution, CuSO₄ fractionation, copper-chelating column chromatography, S-Sepharose column chromatography. Specific activity of purified IFN-α2 was 1.6 × 10^9 IU/㎎ protein and the degree of purification was 94 fold from the starting material. Purified IFN-α2 was formed a single band on SDS-PAGE under reducing condition and also on non-reducing condition. Its molecular weight was estimated to be 18,000 dalton and the isoelectric point of purified IFN-α2 was 6.0. Purity of the recombinant IFN-α2 was better than 99% by densitometric analysis of SDS-PAGE.