Uchańska-Ziegler B, Wernet P, Liangru S, Ziegler A
FEBS Lett. 1984 Oct 1;175(2):279-83. doi: 10.1016/0014-5793(84)80751-6.
The possible molecular heterogeneity of human transferrin receptors was analyzed using two murine monoclonal antibodies, Tü15 and Tü67. Both reagents precipitated from lysates of 125I-labeled HL-60 cells a major component of 88 kDa which could be identified as the transferrin receptor by comparison with the proteins detected by monoclonal antibody OKT9. Although sequential immunoprecipitations appeared to demonstrate molecular heterogeneity of transferrin receptors, since the Tü15-reactive species were fully included in the Tü67-positive population, but not vice versa, the possible association of Tü15-reactive molecules with transferrin receptor is also discussed.
利用两种鼠单克隆抗体Tü15和Tü67分析了人转铁蛋白受体可能存在的分子异质性。两种试剂均从125I标记的HL-60细胞裂解物中沉淀出一种88 kDa的主要成分,通过与单克隆抗体OKT9检测到的蛋白质进行比较,该成分可被鉴定为转铁蛋白受体。尽管连续免疫沉淀似乎证明了转铁蛋白受体的分子异质性,因为Tü15反应性物种完全包含在Tü67阳性群体中,但反之则不然,本文还讨论了Tü15反应性分子与转铁蛋白受体的可能关联。