Perosa F, Luccarelli G, Neri M, Dammacco F
Department of Biomedical Sciences and Human Oncology (DIMO), University of Bari Medical School, Italy.
J Immunol Methods. 1997 Apr 25;203(2):153-5. doi: 10.1016/s0022-1759(97)00021-5.
Seven out of ten Fab (F(ab')2/Fab') preparations derived from purified human myeloma IgG showed a substantial binding to protein G-Sepharose. Subclass analysis revealed that the 7 protein G-reactive Fabs included 3 IgG1, 2 IgG3 and 2 IgG4 Fabs, whereas the remaining 3 which were not adsorbed were IgG2 Fab. Incubation of protein G-Sepharose with non-saturating amounts of 4 Fab preparations, representative of all IgG subclasses, showed that gamma 1, gamma 3 and gamma 4 Fabs adsorbed from 26 to 28.3%, whereas 80% of gamma 2 Fab was left in the supernatant after adsorption. These results indicate that human IgG2 lack PG-specific Fab-associated reactive site(s).
从纯化的人骨髓瘤IgG中获得的十分之七的Fab（F(ab')2/Fab'）制剂与蛋白G-琼脂糖有大量结合。亚类分析显示，7种与蛋白G反应的Fab包括3种IgG1、2种IgG3和2种IgG4 Fab，而其余未被吸附的3种是IgG2 Fab。用代表所有IgG亚类的非饱和量的4种Fab制剂孵育蛋白G-琼脂糖，结果显示γ1、γ3和γ4 Fab的吸附率为26%至28.3%，而吸附后80%的γ2 Fab留在上清液中。这些结果表明人IgG2缺乏与蛋白G特异性Fab相关的反应位点。
