The role of ceruloplasmin in Fe(III)—transferrin formation in vitro
The role of ceruloplasmin in Fe(III)—transferrin formation in vitro
复制标题
铜蓝蛋白在体外 Fe(III)-转铁蛋白形成中的作用
DOI：
10.1016/0014-5793(80)80089-5
复制
发表时间：
1980
期刊：
影响因子：
3.5
通讯作者：
R. Crichton
中科院分区：
文献类型：
--
作者：
J. Mareschal;R. Rama;R. Crichton
铜蓝蛋白对铁动员的演示(EC 1.12。L和对铜缺乏动物的研究[2]强烈表明铜蓝蛋白是铜和铁代谢之间的直接分子联系。铜蓝蛋白的氧化铁酶活性在文献[3]中首次被观察到，并证实了铜蓝蛋白的氧化酶活性对铁的活性大于对其他底物的活性。因此，铜蓝蛋白催化铁的氧化，是铁(III)-转铁蛋白形成途径中必不可少的一步。然而，可以引用几个观察结果来反对这一理论：(I)没有证据表明威尔逊病患者存在铁动员缺陷[5]；(Ii)与相应的人或猪蛋白相比，大鼠铜蓝蛋白显示出相对较低的铁氧合酶活性[6]；(Iii)人和大鼠铜蓝蛋白在生理pH下的铁氧合酶活性仅为其在pH 6.7和6.0时活性的-1/7。
The demonstration of iron mobilization by ceruloplasmin (EC 1.12. 3.1) in perfused dog liver [l] and studies on copper-deficient animals [2] strongly suggest that ceruloplasmin is a direct molecular link between copper and iron metabolism. The ferroxidase activity of ceruloplasmin was first observed in [3] with the confirmation [4] that the oxidase activity of ceruloplasmin was greater for iron than for any other substrate. Thus, it was suggested that the ceruloplasmin catalyzed oxidation of iron and was an essential step on the pathway of Fe (III)-transferrin formation. However, several observations may be cited against this theory:(i) There is no evidence for defective iron mobilization in patients with Wilson’s disease [5];(ii) Rat ceruloplasmin exhibits a relatively low ferroxidase activity when compared to the corresponding human or pig proteins [6];(iii) The ferroxidase activity of human and rat ceruloplasmin at physiological pH is only-1/7th of the activity, that it has at pH 6.7 and 6.0, respectively