Kasuga M, Karlsson F A, Kahn C R
Science. 1982 Jan 8;215(4529):185-7. doi: 10.1126/science.7031900.
Cultured human lymphocytes and rat hepatoma cells were labeled with [32P]orthophosphate and the insulin receptor subunits identified by immunoprecipitation and sodium dodecyl sulfate-gel electrophoreses. In both cell types the 95,000-dalton (beta) subunit of the insulin receptor was selectively phosphorylated. Phosphorylation was specifically stimulated by insulin in a dose-dependent fashion after 1 and 15 minutes of hormone treatment, whereas human growth hormone was without effect. This phosphorylation may be a very early event in insulin action.
用[32P]正磷酸盐标记培养的人淋巴细胞和大鼠肝癌细胞，通过免疫沉淀和十二烷基硫酸钠-凝胶电泳鉴定胰岛素受体亚基。在这两种细胞类型中，胰岛素受体的95,000道尔顿（β）亚基都被选择性磷酸化。激素处理1分钟和15分钟后，胰岛素以剂量依赖的方式特异性刺激磷酸化，而人生长激素则无此作用。这种磷酸化可能是胰岛素作用中非常早期的事件。
