Scutari G, Branca D, Pastorio C
Boll Soc Ital Biol Sper. 1979 Mar 30;55(6):517-22.
Membranes from human erythrocytes exhibit a marked decrease of the ouabain-insensitive ATPase activity and of the total membrane thiol content after treatment with diazenedicarboxylic acid bis(N,N-dimethylamide) (diamide). These effects increase with diamide concentrations up to 2-2.5 mM and are persistent after removal of the reagent. Treatment with 2,3-dihydroxy-1,4-dithiolbutane (dithioerythritol or DTE) reduced glutathione or 2-mercaptoethanol partially but significantly restores at about the same extent the ouabain-insensitive ATPase activity. These results indicate that the perturbation of the ATPase microenvironment caused by membrane thiol oxidation is at good extent responsible for alterations of the divalent cation-dependent ATPase activity.
在用二氮杂环二甲酸双（N，N - 二甲基酰胺）（二酰胺）处理后，人红细胞膜上的哇巴因不敏感ATP酶活性和总膜硫醇含量显著降低。这些效应随着二酰胺浓度增加至2 - 2.5 mM而增强，并且在去除试剂后仍然存在。用2,3 - 二羟基 - 1,4 - 二硫代丁烷（二硫苏糖醇或DTE）、还原型谷胱甘肽或2 - 巯基乙醇处理可部分但显著地在大致相同程度上恢复哇巴因不敏感ATP酶活性。这些结果表明，膜硫醇氧化引起的ATP酶微环境扰动在很大程度上导致了二价阳离子依赖性ATP酶活性的改变。
