Polypeptide-Fe is the hemoglobin that is purified highly from animal blood. It is an active material obtained by connecting heme with a different-length peptide section after physical and chemical processing. Polypeptide-Fe is non-toxic to the human body, does not have the side effects, and namely has iron enhancement function. Nitroblue tetrazolium staining showed that it retained the superoxide radical scavenging activity of hemoglobin. Polypeptide-Fe achieves the elimination of free radical by degradations of the polypeptide connected to iron. Oxidative stress has been considered to play an important role in the pathogenesis of iron-deficiency anemia. The primary free radicals in most of biological system are the superoxide anion, hydrogen peroxide, and the hydroxyl free radical. We performed experiments to detect the clearance ability on these three free radicals and maleic dialdehyde by polypeptide-Fe. Results of the present study showed that polypeptide-Fe had strong antioxidant ability and it may provide some useful information relevant to an additional contribution to the treatment of iron-deficiency anemia in future.