Jellinck P H, Perry M, Løvsted J, Newcombe A M
J Steroid Biochem. 1985 Jun;22(6):699-704. doi: 10.1016/0022-4731(85)90274-2.
The activation of 14C-labeled estradiol by "true" and "pseudo" peroxidases to form conjugates and other products was compared in four model systems using H2O2, glutathione, Mn2+ or irradiated riboflavin. Albumin was used as acceptor except in the glutathione system. The binding of estradiol to glutathione in the presence of the true peroxidases, lacto- or uterine peroxidase (no H2O2 added), was also examined and the conditions shown to differ from those required with the pseudoperoxidases, microperoxidase or trypsin-digested cytochrome c. The conjugates were purified by chromatography after elution from Amberlite XAD-2 and the relative amounts of these products assessed by autoradiography. The ratio of steroid to glutathione in the main water-soluble metabolite formed with lactoperoxidase was found to be approx 1:1 in a double label experiment with [14C]estradiol and [3H]glutathione. It was also shown, using estradiol labeled with 3H in different positions of the steroid molecule, that lactoperoxidase acts non-specifically in catalyzing the formation of glutathionyl conjugates as indicated by the release of 3H2O. The possible role of peroxidase and glutathione in the metabolism of estrogens and in the formation of artifactual products is discussed.
在四个使用过氧化氢、谷胱甘肽、锰离子或辐照核黄素的模型系统中，比较了“真”过氧化物酶和“假”过氧化物酶对14C标记雌二醇的激活作用，以形成共轭物和其他产物。除了在谷胱甘肽系统中，白蛋白用作受体。还研究了在真过氧化物酶（乳过氧化物酶或子宫过氧化物酶，不添加过氧化氢）存在下雌二醇与谷胱甘肽的结合情况，并表明其条件与假过氧化物酶、微过氧化物酶或胰蛋白酶消化的细胞色素c所需的条件不同。共轭物从Amberlite XAD - 2洗脱后通过色谱法纯化，并通过放射自显影评估这些产物的相对量。在用[14C]雌二醇和[3H]谷胱甘肽进行的双标记实验中，发现与乳过氧化物酶形成的主要水溶性代谢物中类固醇与谷胱甘肽的比例约为1:1。还使用在类固醇分子不同位置标记有3H的雌二醇表明，乳过氧化物酶在催化谷胱甘肽共轭物形成时具有非特异性作用，这由3H2O的释放表明。讨论了过氧化物酶和谷胱甘肽在雌激素代谢以及人工产物形成中的可能作用。
