Usui H, Yoshikawa K, Imazu M, Tsukamoto H, Takeda M
FEBS Lett. 1985 May 6;184(1):60-4. doi: 10.1016/0014-5793(85)80653-0.
When membrane fractions from mouse liver, Ehrlich ascites tumor and MH134 hepatoma were incubated with [gamma-32P]ATP at 0 degree C in the presence of MnCl2, ZnCl2 and NaVO3, proteins were phosphorylated on tyrosines to a larger extent in liver membranes than in tumor membranes. Separation of labelled proteins by SDS-gel electrophoresis showed phosphorylated alkali-resistant bands of 170, 140, 130, 80, 56, 53 and 46 kDa proteins in Ehrlich ascites tumor membranes; liver membranes exhibited more strongly phosphorylated bands of 170, 56, 53 and 46 kDa proteins. Epidermal growth factor stimulated the tyrosine phosphorylation of only a 170 kDa protein, which was more significant in liver membranes. Liver membranes exhibited slightly higher levels of tyrosine protein kinase activity compared to tumor membranes.
当将来自小鼠肝脏、艾氏腹水瘤和MH134肝癌的膜组分在0℃下于MnCl2、ZnCl2和NaVO3存在的情况下与[γ-32P]ATP一起温育时,肝脏膜中的蛋白质酪氨酸磷酸化程度比肿瘤膜中的更大。通过SDS-凝胶电泳分离标记的蛋白质显示,艾氏腹水瘤膜中有170、140、130、80、56、53和46 kDa蛋白质的磷酸化抗碱条带;肝脏膜中170、56、53和46 kDa蛋白质的条带磷酸化更强。表皮生长因子仅刺激一种170 kDa蛋白质的酪氨酸磷酸化,这在肝脏膜中更显著。与肿瘤膜相比,肝脏膜表现出略高水平的酪氨酸蛋白激酶活性。