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Iranian Journal of Public Health. 2005; 34 (4): 58-66
in English | IMEMR | ID: emr-71135

ABSTRACT

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


Subject(s)
Erythrocytes/enzymology , Copper , Zinc
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