大蒜细胞溶质中超氧化物歧化酶的性质研究

Study on the Properties of Superoxide Dismutase from Allium sativum Plasma

利用热变性、等电点沉淀和DEAE -纤维素柱层析分离纯化大蒜细胞溶质中的超氧化物歧化酶 ,并对其性质进行了研究。结果表明 ,温度 40～ 6 0℃、pH4～ 9范围内酶的活性稳定 ,对KCN和H2 O2 敏感 ,紫外光区的吸收峰在 2 5 8nm ,可见光区的吸收峰在 6 80nm ,表明酶的类型为Cu·Zn SOD。

A superoxide dismutase from Allium sativum plasma has been isolated and purified by the heat treatment, sedimentation with isoelectric point and chromatograph on DEAE-cellulose, and it's property was studied. The study shows that the enzymatic activity is stable within the temperature 40～60℃ and pH 4～9, and the enzyme is sensitive to KCN and H 2O 2, the absorption apex exhibits at 258 nm in ultraviolet spectrum and at 680 nm in visible spectra,the facts indicate that the enzyme is copper/zinc SOD.