论文部分内容阅读
我们首次发现的铜锌超氧歧化酶（Ｃｕ２Ｚｎ２ＳＯＤ）与氨基酸等发生直接相互作用的现象，是一种前人未研究过的重要的生化新现象［１］。在此新发现的基础上，本文用ＩＣＰ，ＶＩＳ，ＮＭＲ和酶活性测定等方法，又从不同角度拓展研究了Ｃｕ２Ｚｎ２ＳＯＤ酶与两类不同化合物，即无机氯化钴（ＣｏＣｌ２）、有机组氨酸钴（Ｃｏ（Ⅱ）（Ｈｉｓ）ｎ）的直接相互作用，发现酶活性中心金属离子同样与外加的这两类不同化合物发生相互作用，相应地影响了酶的催化活性。还发现Ｃｏ（Ⅱ）（Ｈｉｓ）ｎ比ＣｏＣｌ２与酶相互作用更强、更快，Ｃｏ（Ⅱ）（Ｈｉｓ）ｎ中的Ｃｏ（Ⅱ）更易进入酶中，更影响了酶的催化活性。
Our first discovery of copper-zinc superoxide dismutase (Cu2Zn2SOD) with amino acids and other direct interaction occurs, is a previously unknown biochemical phenomenon [1]. On the basis of this new discovery, we further studied Cu2Zn2SOD enzyme and two different compounds, namely, inorganic cobalt chloride (CoCl2), organic histidine Cobalt (Co (Ⅱ) (His) n). It was found that the metal ions in the active site also interacted with the added two different compounds, which affected the catalytic activity of the enzyme. It was also found that Co (Ⅱ) (His) n had a stronger and faster interaction with CoCl2 than CoCl2, Co (Ⅱ) (His) n was easier to enter into the enzyme and more affected the catalytic activity of Co (Ⅱ).