By using EPR spectroscopy of spin-labelled bovine serum albumin (BSA), bendazac was shown to prevent the BSA denaturation induced by urea, heat and free radicals produced in the xanthine/xanthine oxidase system. Bendazac did not inhibit the reduction of ferricytochrome c due to the superoxide flux in the above system nor did it possess a significant antioxidant activity on Fe(II) or Fe(III)-induced peroxidation of lecithin liposomes. It is concluded that the scavenger-like activity of bendazac is due to its interaction with protein molecules, rather than free radicals.