In this paper, the superoxide dismutase fromMartianus dermestoidesis purified by the following methods: heat treatment, polyethylene concentration, Sephadex G-75 gel filtration, and DEAE-Sepharose FF ion exchange chromatography. The result shows that the purification multiple is 3.86, the activation yield is 21.89% and the specific activation of the enzyme is 447.6 U/mg. The purified SOD appears to be a sole protein on SDS-PAGE and the molecular weight is estimated to be 40.58 kDa. H2O2can obviously inhibit the enzyme activation and CHCl3-CH3CH2OH only demonstrates basically no inhibitory effect. The type of the dermestoides SOD might be Cu/Zn-SOD. After purification, some enzymatic characterizations of the SOD are studied. The optimum reaction temperature of purified SOD is 50°C. The optimum reaction pH value of purification is 6. The dermestoide SOD has a preferable stability below 50°C and at pH values between 5-8.
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