期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1982
卷号：79
期号：11
页码：3618-3622
DOI：10.1073/pnas.79.11.3618
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A monoclonal antibody was produced against the major structural glycoprotein (P0) of human peripheral nervous system myelin. The hybridomas were generated by fusion of mouse myeloma line NS-1 with spleen cells of C3H mice immunized with purified human peripheral nervous system myelin. Hybridomas were screened by a two-step solid-phase radioimmunoassay, with P0 adsorbed on microtiter plates and with addition of 125I-labeled rabbit anti-mouse IgG as the second step. One derived clone, designated 41G10, bound P0 in the radioimmunoassay 4-fold over the background value obtained by using bovine serum albumin as the negative control antigen. Clone 41G10 was shown by immunofluorescence to bind to frozen sections of human intercostal nerve. Diffuse fluorescent staining occurred uniformly over the entire myelin sheath. The cylindrical axons were unstained. The same pattern of immunofluorescence was noted on rat, hamster, mouse, and rabbit sciatic nerve. Immunofluorescence was abolished when 41G10 was absorbed by P0. The monoclonal antibody 41G10 was absorbed by P0. The monoclonal antibody 41G10 is of the IgM class and activated complement in the presence of myelin vesicles or P0 liposomes but not in their absence.
