Griffin J D, Spangler G, Livingston D M
Proc Natl Acad Sci U S A. 1979 Jun;76(6):2610-4. doi: 10.1073/pnas.76.6.2610.
Incubation of simian virus 40 (SV40) tumor (T) antigen-containing immunoprecipitates with [gamma-32P]ATP results in the incorporation of radioactive phosphate into large T antigen. Highly purified preparations of large T antigen from a SV40-transformed cell line, SV80, are able to catalyze the phosphorylation of a known phosphate acceptor, casein. The kinase activity migrates with large T antigen through multiple purification steps. Sedimentation analysis under non-T-antigen-aggregating conditions reveals that kinase activity and the immunoreactive protein comigrate as a 6S structure. The kinase activity of purified preparations of large T antigen can be specifically adsorbed to solid-phase anti-T IgG, and partially purified T antigen from a SV40 tsA transformation is thermolabile in its ability to phosphorylate casein when compared to comparably purified wild-type T antigen. These observations indicate that the SV40 large T antigen is closely associated with protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) activity.
用[γ-32P]ATP孵育含猿猴病毒40（SV40）肿瘤（T）抗原的免疫沉淀物，会使放射性磷酸盐掺入大T抗原中。从SV40转化细胞系SV80中高度纯化的大T抗原制剂，能够催化已知的磷酸盐受体酪蛋白的磷酸化。激酶活性在多个纯化步骤中与大T抗原一起迁移。在非T抗原聚集条件下的沉降分析表明，激酶活性和免疫反应性蛋白以6S结构共同迁移。纯化的大T抗原制剂的激酶活性可特异性吸附到固相抗T IgG上，与同等纯化的野生型T抗原相比，来自SV40 tsA转化的部分纯化T抗原在磷酸化酪蛋白的能力上是热不稳定的。这些观察结果表明，SV40大T抗原与蛋白激酶（ATP：蛋白质磷酸转移酶，EC 2.7.1.37）活性密切相关。
Zotero 插件
