兔血铜锌超氧化物歧化酶的纯化及其性质

用乙醇－氯仿处理，丙酮分级沉淀，ＤＥＡＥ－纤维层析等方法，从兔血红细胞中纯化出铜锌超氧化物歧化酶，产率为５１％，比活力为１２４３０ｕ／ｍｇ．该酶经冷冻干燥后呈淡蓝色，天然状态，下该酶的分子量约为３００００，由相同的两个亚基组成，紫外扫描表明纯酶在２６５ｎｍ处有最大光吸收值，经聚丙烯酰胺凝胶电泳后，用蛋白染色及ＮＢＴ活性染色均显示出三条带，结果表明用该纯化方法得到的ＳＯＤ为均一性纯酶，氨基酸组成显示

Purification and characterization of a superoxide dismutase from rabbit erythrocytes

Superoxide dismutase (SOD) was purified from rabbit red cells by with McCord and Fridovich method. The Cu-Zn SOD is of a specific acitivity of 12000u/mg. The percentage yield is ca. 51%. The CuZn-SOD is of a pale blue -green color. In its natural form the molecular weight is ca. 30 kDa, consisting of two subunit. The enzyme exhibits an ultraviolet spectrum with a maximum at 265 urn. NBT activity staining and Coomassie Blue staining show the same three bands of the purified enzyme by PAGE. The results show that the CuZn-SOD purified by this method is homogenously pure. The amino acid anlyysis and atom absorption spectrum of the enzyme is very similar to CuZn-SODs reported from other sources. There is no free sulfhydryl group in the enzme.