摘要
本实验用可溶性抗原人 IgM 免疫 BALB/C 小鼠,按常规方法取免疫鼠脾细胞,分别与 NS-1、SP2/0细胞进行融合,ELISA 法筛选只与 IgM 反应阳性的抗体分泌杂交细胞,建立了6株杂交瘤株。经鉴定,此6株细胞分泌的抗体与 IgM 产生特异性反应,而不与其它免疫球蛋白重、轻链及 J 链交叉反应。经免疫电转印的硝酸纤维膜染色只显示分子量为72kD 的电泳带。放射免疫方法检测6个单克隆抗体,可分别识别4个不同的抗原决定簇。此组抗体识别 B 细胞胞浆内及膜表面μ链并可检测乙型病毒性肝炎患者血清中 HB_C-IgM 复合物。本组抗体间彼此加合可提高检测的灵敏性。抗 IgM(μ链)单克隆抗体对研究人 B 细胞的分化、成熟及功能提供了重要途径。
Six lines of hybridoma secreting antibody against the μ chain of human IgM were pro- duced with the conventional hybridoma technique.In ELISA assay,these McAbs specifi- cally reacted with IgM,and no cross reaction was observed with heavy,light or J chain of other immunoglobulins.Only a 72 kD polypeptide was recognized by these antibodies,as estimated by Southern-blotting.Radioimmunoassay indicated that these antibodies recognized 4 different antigenic determinants of the μ chain.The use of these antibodies in studying human B cell differentiation and detecting specific IgM to infectious pathogens such as HBc in the sera of patients with infectious diseases was also discussed.
出处
《军事医学科学院院刊》
CSCD
北大核心
1990年第2期123-128,共6页
Bulletin of the Academy of Military Medical Sciences
基金
自然科学基金资助课题
