摘要：The human erythrocyte is a rich raw material for the purification of Cu-Zn superoxide dismutase (SOD). We applied a simple and rapid procedure for the purification of SOD from human erythrocytes by ion exchange chromatography. The purified SOD had a specific activity of 2285.6 u/mg protein and gave a single band on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS) and each of its to subunit has a molecular weight about 18600 daltons (SOD molecular weight is 37200 daltons).The physicochemical properties of the enzyme obtained by this method are identical to those of the native protein.This procedure appears, therefore, to be a convenient and easily method for isolating this enzyme.
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