Hwang D L, Tay Y C, Barseghian G, Roitman A, Lev-Ran A
J Recept Res. 1985;5(5-6):367-80. doi: 10.3109/10799898509041888.
Triton X-100 strongly affects the receptor binding and autophosphorylation of insulin and epidermal growth factor (EGF) in rat liver Golgi fractions and partially purified microsomal receptors. At concentration 0.05% Triton X-100 decreased the insulin receptor binding by 15% and the EGF receptor binding by 70% as compared to controls. In contrast, 0.05% Triton X-100 increased insulin-stimulated receptor autophosphorylation by more than 370% as compared to 87% in the control. Similarly, the same concentration of Triton X-100 increased the EGF-stimulated receptor phosphorylation by 65% as compared to 14% in the control. EGF receptor binding was more sensitive to the treatment of Triton. At Triton concentrations 0.2% or more, the EGF receptor binding was totally abolished while the insulin receptor binding was decreased by 50%. On the other hand, the activity of ligand-stimulated receptor phosphorylation of both insulin and EGF receptors was only slightly decreased in the presence of 0.2% Triton.
曲拉通X-100对大鼠肝脏高尔基体组分和部分纯化的微粒体受体中胰岛素及表皮生长因子（EGF）的受体结合和自身磷酸化有强烈影响。在浓度为0.05%时，与对照组相比，曲拉通X-100使胰岛素受体结合减少了15%，使EGF受体结合减少了70%。相反，与对照组中87%相比，0.05%的曲拉通X-100使胰岛素刺激的受体自身磷酸化增加了370%以上。同样，相同浓度的曲拉通X-100使EGF刺激的受体磷酸化增加了65%，而对照组中为14%。EGF受体结合对曲拉通处理更为敏感。在曲拉通浓度为0.2%或更高时，EGF受体结合完全被消除，而胰岛素受体结合减少了50%。另一方面，在存在0.2%曲拉通的情况下，胰岛素和EGF受体的配体刺激受体磷酸化活性仅略有下降。
