Suwa K, Nakano M
Proc Soc Exp Biol Med. 1975 Nov;150(2):401-6. doi: 10.3181/00379727-150-39044.
A lipoprotein present in trypsin-treated microsomes can be oxidized with formation of malondialdehyde in a system which contains NADPH, ferric ion-ADP complex, NADPH-cytochrome c reductase and a factor. This factor, a mixture of peptides, can be isolated from hepatic microsomes by trypsin digestion and successive gel filtration through Sephadex G-100 and G-25 columns. Lipid peroxidation in this system catalyzes the deiodination of thyroxine, as does NADPH-dependent lipid peroxidation in fresh hepatic microsomes. Thyroxine inhibits lipid peroxidation as it is deiodinated in this system.
在含有烟酰胺腺嘌呤二核苷酸磷酸（NADPH）、铁离子 - 二磷酸腺苷（ADP）复合物、NADPH - 细胞色素c还原酶和一种因子的体系中，经胰蛋白酶处理的微粒体中存在的一种脂蛋白可被氧化并生成丙二醛。这种因子是一种肽混合物，可通过胰蛋白酶消化，然后依次通过葡聚糖凝胶G - 100和G - 25柱进行凝胶过滤，从肝微粒体中分离出来。该体系中的脂质过氧化作用催化甲状腺素的脱碘反应，新鲜肝微粒体中依赖NADPH的脂质过氧化作用也能催化此反应。在该体系中，甲状腺素在脱碘时会抑制脂质过氧化作用。
