Liu F T, Katz D H
Hybridoma. 1984 Fall;3(3):277-85. doi: 10.1089/hyb.1984.3.277.
In order to obtain monoclonal IgE antibody specific for the major allergens in ragweed pollen extracts, hybridomas were constructed from spleens of mice immunized with ragweed antigen E (AgE). Two hybridomas were selected for thorough study, both secreting antibodies of the IgE class. Large quantities of IgE antibodies were isolated by affinity purification using Sepharose 4B conjugated with ragweed pollen proteins (Fraction A). Both MAbs were found to bind to a high molecular weight and heterogeneous population of proteins, but not to monomeric AgE as demonstrated by protein blot analysis. It is suspected that both MAbs react with low affinity with AgE determinants and binding could be demonstrated only with aggregated forms of AgE. Although the specific antigens with which they react are unknown, these monoclonal IgE antibodies should be useful reagents, complementing the previously obtained monoclonal anti-dinitrophenyl IgE antibody, for studying various aspects of the mouse and human IgE antibody systems.
为了获得对豚草花粉提取物中主要过敏原具有特异性的单克隆IgE抗体，用豚草抗原E（AgE）免疫小鼠，从其脾脏构建杂交瘤。选择了两个杂交瘤进行深入研究，二者均分泌IgE类抗体。使用与豚草花粉蛋白偶联的琼脂糖4B（组分A）通过亲和纯化分离出大量的IgE抗体。蛋白质印迹分析表明，两种单克隆抗体均能与高分子量且异质的蛋白质群体结合，但不与单体AgE结合。据推测，两种单克隆抗体与AgE决定簇的亲和力较低，只有与聚集形式的AgE结合才能得到证实。尽管与之反应的特异性抗原尚不清楚，但这些单克隆IgE抗体应是有用的试剂，可补充先前获得的单克隆抗二硝基苯基IgE抗体，用于研究小鼠和人类IgE抗体系统的各个方面。
