人超氧化物歧化酶的研制

THE PREPARATION OF SUPEROXIDE DISMUTASE FROM HUMAN ERYTHROCYTES

从新鲜人红细胞中提取的超氧化物歧化酶(SOD)是用DEAE-纤维素和Sephadex G_(75)两次柱层析纯化,同时用测定抑制率来监测SOD的活性峰。纯化后的SOD紫外吸收光谱的最大吸收峰在270～275 nm范围内,聚丙稀酰胺凝胶圆盘电泳得到3个蛋白带,与NBT还原反应得到的活性带位置一致,分子量分别为41 687、31 623、15 136。生物活性为3300 umits/mg蛋白,每克分子SOD含Cu、Zn均为2克分子。

Superoxide dismutase was prepared from human crythrocytes. The sample was purified using a DEAE-cellulose column and chromatography on Sephadex G-75. During purification the produce determined the protein peak and SOD active peak at the same time to decide the SOD was present. The enzyme exhibited an ultraviolet absorption spectra with a maximum at 270-275 nm. Polyacrylamide disc gel electrophoresis revealed three bands which were in dose agreement with the active bands by reduction of NBT. The molecular weight was 41687, 31623 and 15136. The specific activity of human SOD possessed 3300 units per mg It contained 2 eq of Cu, Zn per mole of enzyme, respectively.