Zegers J M, Ballieux R E, van Loghem E
Scand J Immunol. 1975;4(2):161-9. doi: 10.1111/j.1365-3083.1975.tb02613.x.
Earlier studies on antisera against Fab of pooled human IgG and IgA myeloma proteins disclosed the presence of class-specific Fd antibodies, the demonstration of which required interaction of heavy and light chains. To extend our knowledge about the antigenic structure of the Fd fragment of human immunoglobulins, antisera were prepared in rabbits against gamma chains of pooled IgG and of four IgG1 myeloma proteins, and Fd gamma fragment and a cyanogen bromide-produced CH1 preparation of an IgG1 myeloma protein, and an Fd' alpha fragment of an IgA1 myeloma protein. No antigenic determinants exclusively confined to the CH1 region of intact human IgG could be demonstrated with these antisera. The antigenic structure of CH1 intact immunoglobulins may thus only be defined by light-chain-dependent determinants.
早期针对人IgG和IgA骨髓瘤蛋白混合物Fab的抗血清研究揭示了类特异性Fd抗体的存在,其证明需要重链和轻链的相互作用。为了扩展我们对人免疫球蛋白Fd片段抗原结构的认识,用兔制备了针对IgG混合物γ链、四种IgG1骨髓瘤蛋白γ链、Fdγ片段、一种IgG1骨髓瘤蛋白经溴化氰处理产生的CH1制剂以及一种IgA1骨髓瘤蛋白的Fd'α片段的抗血清。用这些抗血清未能证明完整人IgG中仅局限于CH1区域的抗原决定簇。因此,完整免疫球蛋白CH1的抗原结构可能仅由轻链依赖性决定簇来定义。