来自反硝化副球菌的一种含锰超氧化物歧化酶。
A manganese-containing superoxide dismutase from Paracoccus denitrificans.
作者信息
Terech A, Vignais P M
出版信息
Biochim Biophys Acta. 1981 Feb 13;657(2):411-24. doi: 10.1016/0005-2744(81)90327-2.
A cyanide-insensitive superoxide dismutase (superoxide: superoxide dismutase EC 1.15.1.1) has been isolated from Paracoccus denitrificans, purified to homogeneity and characterized. It is a soluble, manganese-containing protein with an apparent molecular weight of 41 500 +/- 1000. It is composed of two identical subunits (Mr 23 500) not bound by disulfide linkage. It's isoelectric point is 4.5. The amino acid composition shows strong similarities with other dimeric procaryotic and with tetrameric mitochondrial Mn-superoxide dismutases. The fully active enzyme contained from 1.34 to 2 gatom Mn/mol enzyme.
已从反硝化副球菌中分离出一种对氰化物不敏感的超氧化物歧化酶（超氧化物：超氧化物歧化酶，EC 1.15.1.1），并将其纯化至同质且进行了特性鉴定。它是一种可溶性含锰蛋白，表观分子量为41500±1000。它由两个相同的亚基（Mr 23500）组成，亚基间无二硫键连接。其等电点为4.5。氨基酸组成与其他二聚体原核生物以及四聚体线粒体锰超氧化物歧化酶有很强的相似性。完全活性的酶每摩尔酶含有1.34至2克原子锰。
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