Nonenzymatically glycated human serum albumin and glycated poly-lysine(Lys) in vitro brought about the reduction of nitroblue tetrazolium and ferricytochrome c at pH 9.06 and pH 7.8, respectively. This reduction was inhibited partially by superoxide dismutase (SOD). Glycated poly-Lys caused the oxidation of NADH in the presence of LDH at pH 7.0 which was completely inhibited by SOD. Glycated material was found to function both as a reductant and an oxidant. The reactivity of glycated material is discussed and a possible mechanism by which superoxide is produced is proposed. Results may give a clue to diabetic complications.