Georgoussi Z, Sotiroudis T G
Biochem Biophys Res Commun. 1985 Feb 15;126(3):1196-200. doi: 10.1016/0006-291x(85)90312-2.
The Ca2+-dependent ATPase activity of sarcoplasmic reticulum was inhibited when membrane vesicles were incubated at 0 degree C in presence of thiols. 2-mercaptoethanol was the most effective inhibitor from the thiols tested. The effect of 2-mercaptoethanol on the ATPase activity was biphasic; enzyme inhibition originally increased and then decreased with increasing thiol concentration. The inhibitory action of this thiol was significantly higher at low membrane concentrations and the rate of inactivation at 22 degrees C was considerably lower than that at 0 degree C. Ca2+-ATPase previously inhibited by 2-mercaptoethanol was partially reactivated by incubation with periodate.
当膜囊泡在0℃下于硫醇存在的情况下孵育时，肌浆网的Ca2+依赖性ATP酶活性受到抑制。在测试的硫醇中，2-巯基乙醇是最有效的抑制剂。2-巯基乙醇对ATP酶活性的影响是双相的；酶抑制最初随着硫醇浓度的增加而增加，然后下降。这种硫醇的抑制作用在低膜浓度时明显更高，并且在22℃下的失活速率明显低于在0℃时。先前被2-巯基乙醇抑制的Ca2+-ATP酶通过与高碘酸盐孵育而部分重新激活。
