Poláková K, Karpatová M
Cancer Research Institute, Slovak Academy of Sciences, Bratislava.
Neoplasma. 1991;38(1):21-31.
A new monoclonal antibody TR-19 (IgG2a) directed to the human transferrin receptor (CD71) was prepared after immunization of BALB/c mice with human non-T, non-B ALL cell line REH-6. This monoclonal antibody (mAb) reacted in immunofluorescence with all human cell lines tested. The reactivity with human peripheral blood leukocytes was observed only after stimulation with phytohemagglutinin (PHA). The protein precipitated by mAb TR-19 has an apparent molecular weight of 180 kDa under nonreducing and 90 kDa under reducing conditions. Sequential immunoprecipitation showed that mAb TR-19 recognizes the same antigen as the reference anti-transferrin receptor mAb OKT9. The mAb TR-19 coprecipitates the radioiodinated transferrin as a complex with its receptor. The mAb TR-19 with other three mAbs (OKT9, 5E9 and MEM-75) was used in the topographic study of the transferrin receptor. By competitive binding radioimmunoassay it was found that these mAbs recognize two distinct antigenic sites: One is specified by mAbs TR-19 and OKT9 and the second by mAbs 5E9 and MEM-75.
用人非T、非B急性淋巴细胞白血病细胞系REH-6免疫BALB/c小鼠后，制备了一种针对人转铁蛋白受体（CD71）的新型单克隆抗体TR-19（IgG2a）。该单克隆抗体在免疫荧光实验中与所有测试的人细胞系均发生反应。仅在用植物血凝素（PHA）刺激后人外周血白细胞才表现出反应性。在非还原条件下，TR-19单克隆抗体沉淀的蛋白表观分子量为180 kDa，在还原条件下为90 kDa。连续免疫沉淀表明，TR-19单克隆抗体与参比抗转铁蛋白受体单克隆抗体OKT9识别相同抗原。TR-19单克隆抗体能使放射性碘化转铁蛋白与其受体形成复合物而共同沉淀。TR-19单克隆抗体与其他三种单克隆抗体（OKT9、5E9和MEM-75）用于转铁蛋白受体的定位研究。通过竞争性结合放射免疫分析发现，这些单克隆抗体识别两个不同的抗原位点：一个由TR-19和OKT9单克隆抗体识别，另一个由5E9和MEM-75单克隆抗体识别。
