Recombinant human IFN-γ from Chinese Han nationality,overexpressed in E.Coli, was found to accumulate in cytoplasmicinclusion bodies.After washing, the inclusion bodies were dissolved in 8 mol/L urea. Under the denatured states, the recombinant human IFN-γ from Chinese Han nationality was purified by size-exclusion chromatography and ion-exchange chromatography.The final yielded product was of high purity(96.87%) and exhibited the mass of molecule 17.32 ku analyzed by mass spectrometry.The renatured IFN-γ, which was refolded by diluting, had specific antiviral activity of 5.5×10⁵ U/mg. The sequence of 16 amino acid residues from NH₂-terminus of the protein was determined and was found to agree with that of hIFN-γ reported by Gray. The composition of amino acids of the protein was analyzed. The result had good agreement with that deduced from cDNA of IFN-γ from Chinese Han nationality.