Bolann B J, Ulvik R J
Laboratory of Clinical Biochemistry, University of Bergen, Haukeland Hospital, Norway.
FEBS Lett. 1993 Aug 16;328(3):263-7. doi: 10.1016/0014-5793(93)80940-v.
The redox interaction between O2.- and ferritin cannot solely be regarded as as a Fe(II) release reaction. We demonstrate that native copper bound to horse spleen ferritin and apoferritin, stimulated the decay of O2.- in a catalytic reaction. Copper was determined by atomic absorption spectrophotometry. Decay of O2.- was monitored spectrophotometrically as the decrease in (A250-A360) at pH 9.5. The catalytic effect was linearly related to the copper content of the protein. Ferritin copper was less efficient than equimolar CuCl2, and iron-poor ferritin was more efficient than iron-rich ferritin. The results support a direct antioxidant function of ferritin.
超氧阴离子（O2.-）与铁蛋白之间的氧化还原相互作用不能仅仅被视为铁（II）释放反应。我们证明，与马脾铁蛋白和脱铁铁蛋白结合的天然铜，在催化反应中刺激了超氧阴离子（O2.-）的衰减。通过原子吸收分光光度法测定铜含量。在pH 9.5条件下，通过分光光度法监测超氧阴离子（O2.-）的衰减，即（A250 - A360）的降低。催化作用与蛋白质中的铜含量呈线性相关。铁蛋白铜的效率低于等摩尔的氯化铜，贫铁铁蛋白比富铁铁蛋白更有效。这些结果支持了铁蛋白的直接抗氧化功能。
