Maiorino M, Roveri A, Coassin M, Ursini F
Department of Biological Chemistry, University of Padova, Italy.
Biochem Pharmacol. 1988 Jun 1;37(11):2267-71. doi: 10.1016/0006-2952(88)90591-6.
The glutathione peroxidase activity of ebselen (PZ51) was studied using different hydroperoxidic substrates. The single progression curves obtained in the spectrophotometric test were processed by a computer to fit the integrated rate equation that describes the ping pong reaction of the Se glutathione peroxidase. Ebselen catalyzes the GSH peroxidase reaction with a mechanism that appears kinetically identical to the mechanism of the enzymes. The inactivation of the catalytic properties of ebselen by iodoacetate suggests that a selenol moiety is involved. Among the substrates tested, the best hydroperoxidic substrates are the hydroperoxy derivatives of phosphatidyl choline. Ebselen is active also on membrane hydroperoxides as does phospholipid hydroperoxide glutathione peroxidase but not glutathione peroxidase.
使用不同的氢过氧化物底物研究了依布硒啉（PZ51）的谷胱甘肽过氧化物酶活性。通过计算机处理分光光度测试中获得的单进程曲线，以拟合描述硒谷胱甘肽过氧化物酶乒乓反应的积分速率方程。依布硒啉催化谷胱甘肽过氧化物酶反应的机制在动力学上似乎与该酶的机制相同。碘乙酸使依布硒啉的催化特性失活，这表明涉及一个硒醇部分。在所测试的底物中，最佳的氢过氧化物底物是磷脂酰胆碱的氢过氧衍生物。依布硒啉对膜氢过氧化物也有活性，这与磷脂氢过氧化物谷胱甘肽过氧化物酶相同，但与谷胱甘肽过氧化物酶不同。
