Gross H J
Blut. 1985 Aug;51(2):117-22. doi: 10.1007/BF00320120.
A monoclonal antibody D51 has been obtained during immunization against human fetal thymus. The antibody binds to a variety of leukemic cells. This is similar to the staining pattern of the mAb OKT9 and L 5.1, which recognize the transferrin receptor. However, there are some differences. The antibody immunoprecipitates a protein present on Molt-4 cells. Under reducing conditions this protein has a molecular weight of 90 K dalton. Under non-reducing conditions it has a molecular weight of 180 K dalton. This suggests a dimeric structure. The consecutive immunoprecipitation with D51 and OKT9, respectively, demonstrates that both antibodies recognize the structure of the transferrin receptor.
在针对人胎儿胸腺进行免疫接种的过程中获得了一种单克隆抗体D51。该抗体可与多种白血病细胞结合。这与识别转铁蛋白受体的单克隆抗体OKT9和L 5.1的染色模式相似。然而,也存在一些差异。该抗体可免疫沉淀存在于Molt-4细胞上的一种蛋白质。在还原条件下,这种蛋白质的分子量为90千道尔顿。在非还原条件下,其分子量为180千道尔顿。这表明其具有二聚体结构。分别用D51和OKT9进行连续免疫沉淀表明,两种抗体都识别转铁蛋白受体的结构。