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KMID : 0369819950250020145
Jorunal of Korean Pharmaceutical Sciences
1995 Volume.25 No. 2 p.145 ~ p.152
Comparsion of Cu(II)-DISP and Human Recombinant Superoxide Dismutase, an Antioxidant



Abstract
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 10g/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 (15.5hr) compared to native hrSOD (5min).
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.
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