Matzku S, Bröcker E B, Brüggen J, Dippold W G, Tilgen W
Cancer Res. 1986 Aug;46(8):3848-54.
The process of monoclonal antibody (MAb) binding to tumor cells is greatly influenced by the biology of the respective antigen. This was concluded from an analysis of binding and release of MAbs and MAb fragments to melanoma cells at different concentration levels and different temperatures. With an antigen known to be stably expressed at the cell surface (i.e., Mr 97,000 protein) rapid binding of MAbs was observed at both 0 degrees C and 37 degrees C, and this was reversed by treatment with isoosmolar acid buffer. With another group of antigens, MAb binding increased continuously up to considerable levels at 37 degrees C, but not at 0 degrees C. Concomitantly, the portion of radioactive MAb not desorbable by acid buffer treatment increased, pointing to temperature-dependent internalization. With still another group of (glycolipid) antigens, the highest MAb binding was obtained with fixed cells at 0 degrees C. In this situation MAb release was particularly rapid, thus pointing to a shedding process.
单克隆抗体（MAb）与肿瘤细胞的结合过程受相应抗原生物学特性的显著影响。这是通过分析不同浓度水平和不同温度下单克隆抗体及单克隆抗体片段与黑色素瘤细胞的结合和释放得出的结论。对于一种已知在细胞表面稳定表达的抗原（即97,000分子量的蛋白质），在0℃和37℃时均观察到单克隆抗体的快速结合，且用等渗酸性缓冲液处理可使其逆转。对于另一组抗原，单克隆抗体在37℃时的结合持续增加至相当高的水平，但在0℃时则不然。与此同时，经酸性缓冲液处理后不可解吸附的放射性单克隆抗体比例增加，表明存在温度依赖性内化。对于另一组（糖脂）抗原，在0℃下固定细胞时获得最高的单克隆抗体结合。在这种情况下，单克隆抗体的释放特别迅速，从而表明存在脱落过程。
