Berndt J, Hegardt F G, Bové J, Gaumert R, Still J, Cardó M T
Hoppe Seylers Z Physiol Chem. 1976 Sep;357(9):1277-82. doi: 10.1515/bchm2.1976.357.2.1277.
Hydroxymethylglutaryl coenzyme A reductase, the regulatory enzyme of cholesterol biosynthesis, was activated by in-vitro incubation of mouse liver microsomes with an artificial system consisting of Na2SO3, MgCl2 and EDTA. The extent and the time course of the activation were very similar to those observed with a 105 000 x g liver supernatant. Throughout its diurnal rhythm hydroxymethylglutaryl-CoA reductase was activated about threefold, while after cholesterol feeding the extent of activation was diminished but was not abolished. The activation could be inhibited by 0.1M fluoride, indicating that a phosphatase might be involved in the activation process.
羟甲基戊二酰辅酶A还原酶是胆固醇生物合成的调节酶，通过将小鼠肝脏微粒体与由亚硫酸钠、氯化镁和乙二胺四乙酸组成的人工系统进行体外孵育可使其激活。激活的程度和时间进程与用105 000×g肝脏上清液观察到的非常相似。在其昼夜节律中，羟甲基戊二酰辅酶A还原酶被激活约三倍，而喂食胆固醇后激活程度降低但未消除。该激活可被0.1M氟化物抑制，表明磷酸酶可能参与激活过程。
