Requirement of intact human ceruloplasmin for the glutathione‐linked peroxidase activity

FEBS Letters

Park, Seon Young¹  Kim, In Gyu¹ 

[1] Department of Radiation Biology, Environment Radiation Research Group, Korea Atomic Energy Research Institute, P.O. Box 105, Yusong, Taejon 305-600, South Korea

关键词: Human ceruloplasmin;    Glutathione-linked peroxidase;    Proteolytic fragment;    Antioxidant;   

DOI  :  10.1016/S0014-5793(98)01253-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Structural integrity may be needed for the glutathione-linked peroxidase activity of human ceruloplasmin. Intact human ceruloplasmin has a potent peroxidase property to decompose H₂O₂ in the presence of reduced glutathione. However, the fragment of approximately 116 000 Da produced by proteolytic degradation had less than one-third of the glutathione-linked peroxidase activity of intact ceruloplasmin. When further proteolysis occurred, glutathione-linked peroxidase activity of human ceruloplasmin disappeared. In contrast, ceruloplasmin (116 000 Da and <96 000 Da) fragmented by proteolysis significantly removed H₂O₂ irrespective of the presence of reduced glutathione. Although proteolytic fragmentation of ceruloplasmin occurs, the antioxidant activity of ceruloplasmin that prevents DNA strand breaks in a metal-catalyzed reaction system was significantly maintained.

【 授权许可】

Unknown