Wellerson R, Shaw S, Kaplan P
Hybridoma. 1984 Summer;3(2):177-85. doi: 10.1089/hyb.1984.3.177.
Five monoclonal anti-alpha-fetoprotein (AFP) antibodies (IgG1) were isolated from six fusions. They were characterized by examining titration values, affinity constants, isotypes, and epitope binding. Employing an epitope-blocking procedure which was based on the exclusion of like antibodies, four of the five monoclonal antibodies were found to be different. Antibody individuality was further demonstrated by comparison of isoelectric focusing patterns. The existence of four distinct anti-AFP antibodies strongly suggests the presence of at least that many epitopes on the AFP molecule.
从六次融合中分离出五种单克隆抗甲胎蛋白（AFP）抗体（IgG1）。通过检测滴定值、亲和常数、同种型和表位结合对它们进行了表征。采用基于排除同类抗体的表位阻断程序，发现五种单克隆抗体中的四种是不同的。通过比较等电聚焦图谱进一步证明了抗体的个体性。四种不同抗AFP抗体的存在强烈表明AFP分子上至少存在同样多的表位。
