Rest R F, Spitznagel J K
Biochem J. 1977 Aug 15;166(2):145-53. doi: 10.1042/bj1660145.
We have identified two distinct pools of superoxide dismutase in fractions of human peripheral neutrophils obtained by the isopycnic fractionation of homogenates of the latter with linear sucrose gradients. Superoxide dismutase activity, observed with polyacrylamide gels impregnated with Nitro Blue Tetrazolium, was present in: (1) the mitochondrial fraction [density (rho) 1.169g/ml], containing the high-molecular-weight KCN-resistant enzyme, and (2) the cytoplasm fraction, containing the low-molecular-weight KCN-sensitive enzyme. Superoxide dismutase activity, observed with a quantitative assay involving cytochrome c, was present in: (1) the mitochondria, (2) the cytoplasm, and (3) the azurophil-granule fractions (rho=1.206 and 1.222g/ml). No substantial enzyme activity was observed in specific-granule fractions (rho=1.187g/ml) or in the membranous fraction (rho=1.136g/ml) in either assay. The apparent superoxide dismutase activity observed in the azurophil granules with the cytochrome c assay was attributable not to true superoxide dismutase but to myeloperoxidase, an enzyme found solely in the azurophil granules. In the presence of H(2)O(2), human neutrophil myeloperoxidase oxidized ferrocytochrome c. Thus, in the cytochrome c assay for superoxide dismutase, the oxidation of ferrocytochrome c by myeloperoxidase mimicked the inhibition of reduction of ferricytochrome c by superoxide dismutase. When myeloperoxidase was removed from azurophilgranule fractions by specific immuno-affinity chromatography, both myeloperoxidase and apparent superoxide dismutase activities were removed. It is concluded that there is no detectable superoxide dismutase in either the azurophil or specific granules of human neutrophils. Mitochondrial superoxide dismutase, 15% of the total dismutase activity of the cells, occurred only in fractions of density 1.160g/ml, where isocitrate dehydrogenase and cytochrome oxidase were also observed.
我们通过用人外周血中性粒细胞匀浆在线性蔗糖梯度中进行等密度梯度离心,从获得的组分中鉴定出了两类不同的超氧化物歧化酶。在用含氮蓝四唑的聚丙烯酰胺凝胶观察时,超氧化物歧化酶活性存在于:(1)线粒体组分[密度(ρ)1.169g/ml],含有高分子量的抗KCN酶;(2)细胞质组分,含有低分子量的对KCN敏感的酶。在用涉及细胞色素c的定量测定法观察时,超氧化物歧化酶活性存在于:(1)线粒体,(2)细胞质,以及(3)嗜天青颗粒组分(ρ=1.206和1.222g/ml)。在两种测定法中,在特异性颗粒组分(ρ=1.187g/ml)或膜组分(ρ=1.136g/ml)中均未观察到明显的酶活性。在用细胞色素c测定法在嗜天青颗粒中观察到的表观超氧化物歧化酶活性并非归因于真正的超氧化物歧化酶,而是归因于髓过氧化物酶,一种仅在嗜天青颗粒中发现的酶。在有H₂O₂存在的情况下,人中性粒细胞髓过氧化物酶可氧化亚铁细胞色素c。因此,在用于超氧化物歧化酶的细胞色素c测定法中,髓过氧化物酶对亚铁细胞色素c的氧化模拟了超氧化物歧化酶对高铁细胞色素c还原的抑制作用。当通过特异性免疫亲和色谱从嗜天青颗粒组分中去除髓过氧化物酶时,髓过氧化物酶和表观超氧化物歧化酶活性均被去除。得出的结论是,在人中性粒细胞的嗜天青颗粒或特异性颗粒中均未检测到超氧化物歧化酶。线粒体超氧化物歧化酶占细胞总歧化酶活性的15%,仅出现在密度为1.160g/ml的组分中,在该组分中还观察到了异柠檬酸脱氢酶和细胞色素氧化酶。