Moriarity D M, Harper R A, Knowles B B, Savage C R
Hybridoma. 1983;2(3):321-7. doi: 10.1089/hyb.1983.2.321.
A monoclonal antibody directed to a species-specific determinant of human epidermal growth factor (h-EGF) was obtained by fusing murine myeloma cells with BALB/c mouse splenocytes sensitized to h-EGF. This antibody, referred to as 863.D4, did not react with either rat or mouse epidermal growth factor or with 11 other polypeptide hormones tested as shown by solid-phase radioimmunoassay (SPRIA), and immunoprecipitation followed by sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE). Scatchard analysis of the antibody binding to purified h-EGF revealed an apparent equilibrium dissociation constant of 1 X 10(-8) M. The antibody blocked both the binding of h-EGF and h-EGF stimulation of 3H-thymidine incorporation into DNA by greater than 90% in confluent cultures of human foreskin fibroblasts.
通过将鼠骨髓瘤细胞与对人表皮生长因子（h-EGF）致敏的BALB/c小鼠脾细胞融合，获得了一种针对人表皮生长因子物种特异性决定簇的单克隆抗体。这种抗体称为863.D4，通过固相放射免疫分析（SPRIA）以及免疫沉淀后进行十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）显示，它与大鼠或小鼠表皮生长因子以及所测试的其他11种多肽激素均无反应。对该抗体与纯化的h-EGF结合进行的Scatchard分析显示，表观平衡解离常数为1×10⁻⁸M。在人包皮成纤维细胞汇合培养物中，该抗体对h-EGF的结合以及h-EGF刺激的³H-胸腺嘧啶掺入DNA的抑制率均超过90%。
