Pron G, Belehradek J, Mir L M
Laboratoire de Physicochimie et Pharmacologie des Macromolécules Biologiques URA 147 CNRS, U 140 INSERM, Institut Gustave Roussy, Villejuif, France.
Biochem Biophys Res Commun. 1993 Jul 15;194(1):333-7. doi: 10.1006/bbrc.1993.1824.
In this paper, the association of radiolabelled bleomycin on the plasma membrane of DC-3F cells is shown to be saturable, displaying classical features of a ligand-receptor binding. This association corresponds to the presence of 140,000 to 400,000 binding sites at the surface of the cells with a half-saturating concentration of 5 microM. Moreover, using a gel electrophoresis procedure to separate membrane proteins incubated with radiolabelled bleomycin, we demonstrate the existence of a membrane protein of about 250kDa able to specifically bind bleomycin. This membrane bleomycin-binding protein could play a major part in the association of bleomycin with the cells and in its further internalization, a process that has not been elucidated yet.
在本文中，放射性标记的博来霉素与DC - 3F细胞膜的结合显示为可饱和的，呈现出配体 - 受体结合的经典特征。这种结合对应于细胞表面存在140,000至400,000个结合位点，半饱和浓度为5微摩尔。此外，使用凝胶电泳程序分离与放射性标记博来霉素一起孵育的膜蛋白，我们证明存在一种约250kDa的膜蛋白能够特异性结合博来霉素。这种膜博来霉素结合蛋白可能在博来霉素与细胞的结合及其进一步内化过程中起主要作用，而该过程尚未阐明。
