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为测定白细胞介素-2受体(IL-2R)的表达水平,应用 lodogen 法对重组 IL-2(rlL-2)进行~(125)I 标记,以放射配基结合分析法对大鼠脾淋巴细胞表面 IL-2R 进行鉴定。结果表明,rlL-2蛋白质标记率为58.8%,比活度为488.4kBq/μg;~(125)I-IL-2在10～150pmol/L 范围内与淋巴细胞 IL-2R 呈特异性结合,为可饱和的双分子过程,最大结合容量和平衡解离常数分别为10.00±0.68fmol/10~7细胞和73.84±21.06pmol/L。动力学实验表明配基与细胞特异结合具有可逆性,提示可用标记配基对淋巴细胞高亲和力 IL-2R 进行鉴定。
To determine the expression level of interleukin-2 receptor (IL-2R), 125 I-labeled recombinant IL-2 (rlL-2) was detected by lodogen method. Lymphocyte surface IL-2R was identified. The results showed that the labeling rate of rlL-2 protein was 58.8% and the specific activity was 488.4kBq / μg. The specific binding of 125 I-IL-2 to lymphocytes IL-2R in the range of 10-150 pmol / For the saturable bimolecular process, the maximum binding capacity and equilibrium dissociation constants were 10.00 ± 0.68 fmol / 10-7 cells and 73.84 ± 21.06 pmol / L, respectively. Kinetic experiments showed that ligand-cell-specific binding is reversible, suggesting that lymphocyte high-affinity IL-2R could be identified using labeled ligands.