The superoxide dismutase (SOD) mimetic activity of copper complex of 3, 5-disopropylsalicylic acid (Cu(II)-DIPS) was tested and compared to those of human recombinant SOD (hrSOD) and its conjugate form with polyethyleneglycol (PEG) using fer-ricytochrome c reduction assay. Stability constant of Cu(II)-DIPS was measured po-tentiometrically using SCOGS2 program. In the presence of 10 g/L albumin. Cu(II)-DIPS lost most of its SOD mimetic activity. HrSOD was modified with polyethylene glycol (PEG) of M.W. 5000. These conjugates have markedly prolonged plasma half-lives of enzymatic activity (15.5 hr) compared to native hrSOD (5 min). In summary, efficient SOD mimetics should be stable enough not to dissociate in blood by serum protein. HrSOD could have longer half-life by conjugation with inert PEG for sustained SOD effect.