Glycation of recombinant human interferon-gamma (rhIFN-γ) causes conformational alterations of the molecule and results in reduction of its biologic activity. The aim of this study was to find adequate approaches for prevention of glycation in order to obtain a stable recombinant protein with sustained biologic activity. To this end we investigated the effect of seven chemical compounds (acetylsalicylic acid, vitamin B 1 , aminoguanidine, arginine, pyridoxine, pyridoxal 5'-phosphate and

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... mine) on the biologic activity of rhIFN-γ produced in Escherichia coli. The obtained results showed that rhIFN-γ isolated from bacterial cells grown in the presence of 0.1 mM acetylsalicylic acid was the least affected by glycation. It demonstrated high stability in solution and biologic activity of about 2x10 6 IU/mg over three months of storage at -20°C.