Cousin M A, Lando D, Peyrat M A, Soulillou J P
Lymphokine Res. 1985 Fall;4(4):319-30.
We report the characterization of two monoclonal antibodies (mab) directed against unglycosylated human IL2. Mice were immunized with recombinant IL2 (rIL2) and two of the hybridomas obtained (referred to as 15.2 and 17.2) were selected for further analysis. Both 15.2 and 17.2 antibodies bound to recombinant IL2 and weakly to natural IL2 in an enzyme linked immuno assay (ELISA). Both antibodies were very efficient in retaining rIL2 on affinity columns with a yield of 95% purified material after acid elution. In high concentrations both mabs strongly inhibited the growth of CTLL-2 cells induced by the immunizing-rIL2, while the growth of CTLL-2 cells in the presence of natural-IL2 was only slightly inhibited. Neither mab blocked the effect of rat IL2 in this test. Both mabs were used in an immuno-radiometric assay (IRMA) to quantify recombinant IL2. Cross inhibition experiments performed in this last assay indicate that the two mabs recognize two different epitopes on the recombinant IL2 molecule.
我们报告了两种针对未糖基化人白细胞介素2（IL2）的单克隆抗体（mab）的特性。用重组IL2（rIL2）免疫小鼠，并选择获得的两种杂交瘤（称为15.2和17.2）进行进一步分析。在酶联免疫吸附测定（ELISA）中，15.2和17.2抗体均与重组IL2结合，与天然IL2的结合较弱。两种抗体在亲和柱上保留rIL2的效率都很高，酸洗脱后纯化物质的产率为95%。在高浓度下，两种单克隆抗体都强烈抑制免疫用rIL2诱导的CTLL-2细胞生长，而在天然IL2存在的情况下，CTLL-2细胞的生长仅受到轻微抑制。在该试验中，两种单克隆抗体均未阻断大鼠IL2的作用。两种单克隆抗体都用于免疫放射测定（IRMA）以定量重组IL2。在最后一项测定中进行的交叉抑制实验表明，两种单克隆抗体识别重组IL2分子上的两个不同表位。
