Marklund S L
Proc Natl Acad Sci U S A. 1982 Dec;79(24):7634-8. doi: 10.1073/pnas.79.24.7634.
A superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1), distinct from previously known superoxide dismutases, has been isolated from human lung tissue. It is probably of the same nature as a previously demonstrated high molecular weight superoxide dismutating factor in human extracellular fluids. The enzyme has a molecular weight around 135,000 and is composed of four equal noncovalently bound subunits. Each molecule appears to have four copper atoms. No iron or manganese was found in the enzyme. Cyanide inhibits the enzyme efficiently. The enzyme brings about a first-order dismutation of the superoxide radical, the rate constant for the catalyzed reaction being about 1 X 10(9) M-1 s-1 per copper atom. The enzyme has hydrophobic properties. Affinity for various lectins indicates the presence of carbohydrate. Upon chromatography on heparin-Sepharose it is divided into three fractions, one with no, one with weak, and one with strong affinity for heparin.
已从人肺组织中分离出一种超氧化物歧化酶（超氧化物：超氧化物氧化还原酶，EC 1.15.1.1），它与先前已知的超氧化物歧化酶不同。它可能与先前在人细胞外液中证明的高分子量超氧化物歧化因子性质相同。该酶的分子量约为135,000，由四个相等的非共价结合亚基组成。每个分子似乎含有四个铜原子。在该酶中未发现铁或锰。氰化物能有效抑制该酶。该酶能使超氧阴离子发生一级歧化反应，每个铜原子催化反应的速率常数约为1×10⁹ M⁻¹ s⁻¹。该酶具有疏水特性。对各种凝集素的亲和力表明存在碳水化合物。在肝素 - 琼脂糖柱上进行层析时，它被分为三个部分，一个对肝素无亲和力，一个对肝素亲和力弱，一个对肝素亲和力强。
