期刊论文详细信息
FEBS Letters
Inhibition by the protein ceruloplasmin of lipid peroxidation stimulated by an Fe3+—ADP—adriamycin complex
Nakano, Hiroko1  Ogita, Kouji1  Nakano, Minoru1  Gutteridge, John M.C.2 
[1] College of Medical Care and Technology, Gunma University, Maebashi, Gunma, Japan;National Institute for Biological Standards and Control, Holly Hill, Hampstead, London NW3 6RB, England
关键词: Ceruloplasmin;    Superoxide dismutase;    Adriamycin;    Ferroxidase activity;    Lipid peroxidation;    Oxygen radical;   
DOI  :  10.1016/0014-5793(84)80086-1
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
PDF
【 摘 要 】

Self-reduction of an Fe3+—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 Fe2+ to the ferric state. The inhibitory activity of ceruloplasmin towards reactions stimulated by the complex suggests that Fe2+ is formed during the self-reduction process. As expected, the Fe3+—ADP—adriamycin complex stimulated lipid peroxidation in which the Fe2+ moiety was implicated. This stimulation was again effectively prevented by ceruloplasmin but not by superoxide dismutase.

【 授权许可】

Unknown   

【 预 览 】
附件列表
Files Size Format View
RO201912020285149ZK.pdf 423KB PDF download
  文献评价指标  
  下载次数:2次 浏览次数:17次