Hu C H, Tsou C L
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
FEBS Lett. 1991 Sep 23;290(1-2):87-9. doi: 10.1016/0014-5793(91)81232-w.
During the regeneration of native ribonuclease A (RNase) from the disulfide scrambled molecule by protein disulfide isomerase (PDI), the substrate forms a covalent intermediate with the enzyme through disulfide linkage(s). This has been shown by the appearance of a band at the molecular weight position expected in SDS-PAGE at the same time as the increase in RNase activity. The new band decreased when the regeneration of RNase activity approached completion and disappeared by treatment of the reaction mixture with excess dithiothreitol.
在通过蛋白质二硫键异构酶（PDI）从二硫键错配分子再生天然核糖核酸酶A（RNase）的过程中，底物通过二硫键与酶形成共价中间体。这已通过在SDS-PAGE中预期分子量位置出现条带得到证明，同时RNase活性增加。当RNase活性的再生接近完成时，新条带减少，并且通过用过量二硫苏糖醇处理反应混合物使其消失。
