Premium
Thiol‐linked peroxidase activity of human ceruloplasmin
Author(s) -
Kim In Gyu,
Park Seon Young,
Kim Kug Chan,
Yum Jung Joo
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00817-5
Subject(s) - ceruloplasmin , thiol , dithiothreitol , chemistry , peroxidase , biochemistry , glutathione , glutathione peroxidase , antioxidant , oxidase test , enzyme
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/Fe 3+ /O 2 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 H 2 O 2 in the absence of reduced glutathione. On the contrary, ceruloplasmin showed a potent peroxidase ability to destroy H 2 O 2 in the presence of reduced glutathione. In conclusion, the removal of H 2 O 2 by human ceruloplasmin is not simply stoichiometric but thiol‐dependent.