Thiol-linked peroxidase activity of human ceruloplasmin.
Human ceruloplasmin exhibited different antioxidant effects according to the electron donors in a metal-catalyzed oxidation system. Purified ceruloplasmin did not play a significant role in the protection of DNA strand breaks in the ascorbate/Fe3+/O2 system. However, when ascorbates were replaced with a thiol-reducing equivalent such as dithiothreitol, DNA strand breaks were significantly prevented by the same amount of ceruloplasmin. Ceruloplasmin did not catalyze the decomposition of H2O2 in the absence of reduced glutathione. On the contrary, ceruloplasmin showed a potent peroxidase ability to destroy H2O2 in the presence of reduced glutathione. In conclusion, the removal of H2O2 by human ceruloplasmin is not simply stoichiometric but thiol-dependent.
Department of Radiation Biology, Korea Atomic Energy Research Institute, Yusong, Taejon, South Korea. igkim@nanum.kaeri.re.kr
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D000975:Antioxidants / Q000378:metabolism; D002570:Ceruloplasmin / Q000378:metabolism*; D004249:DNA Damage; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D018384:Oxidative Stress; D010544:Peroxidases / Q000378:metabolism*
D000975:Antioxidants; D006861:Hydrogen Peroxide; D010544:Peroxidases; C058652:thiol-dependent peroxidase; D002570:Ceruloplasmin