Végh M, Marton A, Horváth I
Second Institute of Biochemistry, Semmelweis University Medical School, Budapest, Hungary.
Biochim Biophys Acta. 1988 Feb 17;964(2):146-50. doi: 10.1016/0304-4165(88)90160-2.
An NADPH-driven enzymatic reduction of an Fe(III)ADP complex by rat liver microsomes has been demonstrated directly for the first time during the initial phase of lipid peroxidation by using two different analytical methods. The reduction rate increased upon increasing the ratio of ADP to ferric iron. Fe(III)ADP reducing activity of both detergent-solubilized microsomes and purified NADPH:cytochrome-P-450 (cytochrome-c) reductase decreased to about 20% compared to that of the native microsomes. Superoxide dismutase and KCN did not inhibit the reduction.
首次通过两种不同的分析方法直接证明,在脂质过氧化的初始阶段,大鼠肝脏微粒体可由NADPH驱动对Fe(III)ADP复合物进行酶促还原。随着ADP与铁离子比例的增加,还原速率提高。与天然微粒体相比,去污剂增溶的微粒体和纯化的NADPH:细胞色素P-450(细胞色素c)还原酶的Fe(III)ADP还原活性均降至约20%。超氧化物歧化酶和氰化钾不抑制该还原反应。