Lavelle F, Michelson A M
Biochimie. 1975;57(3):375-81. doi: 10.1016/s0300-9084(75)80314-2.
Two different superoxide dismutases have been purified from the luminous fungus Pleurotus olearius. The second enzyme SODm presents structural differences with the first enzyme SODc previously described [5]: it has a molecular weight of 78,000 and is composed of identical subunits (20,000); it contains also two functional Mn atoms. Using an antiserum prepared against SODc, we have shown that there is no cross-reaction between these two proteins. Spectral studies of the first enzyme SODc suggest that the active center contains trivalent manganese Mn-III.
已从发光真菌油橄榄平菇中纯化出两种不同的超氧化物歧化酶。第二种酶SODm与先前描述的第一种酶SODc在结构上存在差异[5]：它的分子量为78,000，由相同的亚基（20,000）组成；它还含有两个功能性锰原子。使用针对SODc制备的抗血清，我们已表明这两种蛋白质之间不存在交叉反应。对第一种酶SODc的光谱研究表明，活性中心含有三价锰Mn-III。
