Nishimura J, Deuel T F
FEBS Lett. 1983 May 30;156(1):130-4. doi: 10.1016/0014-5793(83)80263-4.
The human platelet derived-growth factor (PDGF) is both a potent mitogen and a strong chemoattractant protein for cells involved in inflammation and repair. In seeking mechanisms by which PDGF might initiate specific activities in target cells, it was found that highly purified PDGF stimulates the phosphorylation of an Mr approximately 33000 protein in confluent Swiss mouse 3T3 cells [Biochem. Biophys. Res. Commun. (1981) 103, 355-361]. The Mr approximately 33000 protein has now been recovered in polysomes by differential centrifugation and identified as ribosomal protein S6 by two-dimensional polyacrylamide gel electrophoresis.
人血小板衍生生长因子(PDGF)既是一种强效的有丝分裂原,也是一种对参与炎症和修复的细胞具有强大趋化作用的蛋白质。在探寻PDGF可能在靶细胞中启动特定活性的机制时,发现高度纯化的PDGF可刺激汇合的瑞士小鼠3T3细胞中一种分子量约为33000的蛋白质发生磷酸化[《生物化学与生物物理学研究通讯》(1981年)103, 355 - 361]。现在,通过差速离心已在多核糖体中回收了这种分子量约为33000的蛋白质,并通过二维聚丙烯酰胺凝胶电泳鉴定为核糖体蛋白S6。