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经６５℃加热，硫酸铵分级沉淀，ＳｅｐｈａｄｅｘＧ－１００凝胶过滤和ＤＥ－５２柱层析，从近江牡蛎（ＯｓｔｒｅａｒｉｖｕｌａｒｉｓＧｏｕｌｄ）软体部分提纯了铜锌超氧化物歧化酶（Ｃｕ，Ｚｎ－ＳＯＤ）．对其理化性质鉴定表明，用此法纯化的酶纯度均一．该酶系由两个相同亚基组成的二聚体，分子量２７．９ｋＤ．该酶的紫外吸收峰在２７２．５ｎｍ，红外光谱表现出其氨基酸组成特征，与猪血ＳＯＤ存在差异．该酶在不同的升温速率下及经不同浓度的Ｈ２Ｏ２处理后的稳定性与猪血ＳＯＤ不同．其氨基酸组成与不同来源的同类酶存在差异．
Copper and zinc superoxide dismutase (Cu, Zn-SOD) was purified from the Ostrearivularis Gould software by heating at 65 ° C, ammonium sulfate fractionation, Sephadex G-100 gel filtration and DE-52 column chromatography. Identification of its physical and chemical properties showed that this method of purification of enzyme purity uniformity. This enzyme is a dimer composed of two identical subunits, with a molecular weight of 27.9 kD. The UV absorption peak of the enzyme at 272.5nm, infrared spectroscopy showed its amino acid composition, and pig blood SOD differences. The stability of the enzyme at different heating rates and after treatment with different concentrations of H2O2 is different from that of porcine blood SOD. Their amino acid composition and different sources of similar enzymes are different.