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从猪红细胞中分离纯化到CuZn—SOD。纯化的酶经disc电泳显示为一条蛋白带,酶比活力为每毫克蛋白18000单位。该酶在紫外与可见光区的最大吸收分别为267nm和665nm。经SDS-PAGE测得酶亚基分子量约为16200道尔顿。根据计算,酶亚基由大约151个氨基陵残基组成,不含色氨酸。用DNS法测得N-末端氨基酸是封闭的。等电聚焦电泳得到6条酶蛋白带,其pH值分别为5.70,6.05,6.10,6.30,6.45和6.80.
Purification of CuZn-SOD from pig erythrocytes. The purified enzyme is displayed as a protein band by disc electrophoresis with a specific enzyme activity of 18000 units per milligram of protein. The maximum absorption of the enzyme in the UV and visible regions are 267 nm and 665 nm, respectively. The molecular weight of the enzyme subunit was about 16,200 Daltons as determined by SDS-PAGE. It is calculated that the enzyme subunit consists of about 151 amino acid residues and no tryptophan. The N-terminal amino acids were closed by the DNS method. Isoelectric focusing electrophoresis to obtain six enzyme protein bands, the pH values were 5.70,6.05,6.10,6.30,6.45 and 6.80.