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Human proteins are not routinely expressed at high levels in Escherichia coli for, among other reasons, different codon usage. Several purification procedures have been applied to recover recombinant proteins for further biological characterization. However, the vast majority involve costly chromatography procedures. In the present study, both HuIFNα2b(human interferon α2b) and HuIFNα8were expressed efficiently in E. coli BL21-codonplus-RIL. Subsequently, both recombinant proteins were purified to homogeneity by passive elution from reverse-stained SDS/PAGE gels, a cost-effective purification procedure. After purification, both recovered proteins were biologically active. The HuIFNα8subtype induced 1.46-fold more antiviral activity than HuIFNα2busing Hep-2 human laryngeal carcinoma cell challenged with Mengo virus. [ABSTRACT FROM AUTHOR]