Kitani T, Fujisawa H
Eur J Biochem. 1981 Sep;119(1):177-81. doi: 10.1111/j.1432-1033.1981.tb05591.x.
Ornithine decarboxylase was purified approximately 37000-fold with a 15% yield from livers of rats pretreated with thioacetamide. The specific activity of the final preparation, 1039 units/mg protein, was about four-times higher than the highest yet reported for the rat liver enzyme. The partially purified enzyme was quite labile but the labile enzyme was dramatically stabilized by the presence of either ethylene glycol or Tween 80. The detergent appeared to serve not only stabilization of the enzyme but also renaturation of the denatured enzyme.
从经硫代乙酰胺预处理的大鼠肝脏中纯化出鸟氨酸脱羧酶，纯化倍数约为37000倍，产率为15%。最终制剂的比活性为1039单位/毫克蛋白，比大鼠肝脏酶迄今报道的最高活性约高四倍。部分纯化的酶相当不稳定，但乙二醇或吐温80的存在可显著稳定这种不稳定的酶。去污剂似乎不仅能稳定酶，还能使变性酶复性。
