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ABSTRACTA new approach for improving and scaling up the purification of recombinant human interferon gamma (hIFNγ) expressed in Escherichia coli and accumulated in the form of inclusion bodies was investigated. The new strategy involves denaturation of the inclusion bodies in 7.4M guanidine hydrochloride, loading on a hydrophobic (Octyl-Sepharose) column and elution with urea/ammonium chloride. The method is fast, simple and low in cost. For maximum recovery of the hIFNγ biological activity, an optimization of the refolding step is proposed.