HUMAN COPPER-CONTAINING SUPEROXIDE-DISMUTASE OF HIGH MOLECULAR-WEIGHT
HUMAN COPPER-CONTAINING SUPEROXIDE-DISMUTASE OF HIGH MOLECULAR-WEIGHT
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DOI：
10.1073/pnas.79.24.7634
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发表时间：
1982-01-01
期刊：
影响因子：
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通讯作者：
MARKLUND, SL
中科院分区：
文献类型：
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作者：
MARKLUND, SL
从人肺组织中分离出一种与先前已知的超氧化物歧化酶不同的超氧化物歧化酶。它可能与先前在人类细胞外液中证明的高分子量超氧化物歧化因子具有相同的性质。该酶的分子量约为 135,000，由 4 个相等的非共价结合亚基组成。每个分子似乎都有 4 个 Cu 原子。酶中未发现 Fe 或 Mn。氰化物能有效抑制该酶。该酶引起超氧自由基的一级歧化，催化反应的速率常数约为1倍。每个 Cu 原子 109 M-1 s-1。该酶具有疏水性。对各种凝集素的亲和力表明碳水化合物的存在。在肝素-琼脂糖凝胶上进行层析，将其分为3个级分，1个对肝素无亲和力，1个对肝素弱亲和力，1个对肝素有强亲和力。
A superoxide dismutase distinct from previously known superoxide dismutases, was isolated from human lung tissue. It is probably of the same nature as a previously demonstrated high MW superoxide dismutating factor in human extracellular fluids. The enzyme has a MW around 135,000 and is composed of 4 equal noncovalently bound subunits. Each molecule appears to have 4 Cu atoms. No Fe or Mn 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 .times. 109 M-1 s-1 per Cu atom. The enzyme has hydrophobic properties. Affinity for various lectins indicates the presence of carbohydrate. On chromatography on heparin-Sepharose it is divided into 3 fractions, 1 with no, 1 with weak, and 1 with strong affinity for heparin.