Campen C A, Vale W
Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, California 92037.
Biochem Biophys Res Commun. 1988 Dec 15;157(2):844-9. doi: 10.1016/s0006-291x(88)80326-7.
Recombinant activin A was radioiodinated to a high specific activity with maintenance of bioactivity using the Bolton-Hunter method. The human leukemia cell line K562, known to differentiate in response to activin A, was found to possess high affinity [125I]BH-activin A receptors (Kd approximately 0.13 nM) with a low number of receptors per cell (approximately 600 per cell). This receptor was found to be specific as FSH, LH, GnRH, and TGF-beta 1 do not compete for binding. This is the first description of binding sites for this protein hormone on K562 cells.
使用博尔顿-亨特法将重组激活素A进行放射性碘化,使其具有高比活度并保持生物活性。已知人白血病细胞系K562会对激活素A产生分化反应,研究发现该细胞系具有高亲和力的[125I]BH-激活素A受体(解离常数约为0.13 nM),每个细胞的受体数量较少(约每个细胞600个)。研究发现该受体具有特异性,因为促卵泡激素、促黄体生成素、促性腺激素释放激素和转化生长因子β1不会竞争结合。这是首次描述这种蛋白质激素在K562细胞上的结合位点。