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Inhibition by the protein ceruloplasmin of lipid peroxidation stimulated by an Fe 3+ —ADP—adriamycin complex
Author(s) -
Nakano Hiroko,
Ogita Kouji,
Gutteridge John M.C.,
Nakano Minoru
Publication year - 1984
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 - 10.1016/0014-5793(84)80086-1
Subject(s) - ceruloplasmin , chemistry , superoxide dismutase , lipid peroxidation , biochemistry , ferric , enzyme , hemopexin , heme , inorganic chemistry
Self‐reduction of an Fe 3+ —ADP—adriamycin complex under anaerobic conditions and reduction of ferricytochrome c by the complex under aerobic conditions were strongly inhibited by ceruloplasmin, but not by superoxide dismutase or albumin at the same protein concentration. Ceruloplasmin, a protein with ferroxidase activity, is able to catalyse oxidation of Fe 2+ to the ferric state. The inhibitory activity of ceruloplasmin towards reactions stimulated by the complex suggests that Fe 2+ is formed during the self‐reduction process. As expected, the Fe 3+ —ADP—adriamycin complex stimulated lipid peroxidation in which the Fe 2+ moiety was implicated. This stimulation was again effectively prevented by ceruloplasmin but not by superoxide dismutase.