Hannestad K, Johannessen A
Scand J Immunol. 1976;5(5):541-7. doi: 10.1111/j.1365-3083.1976.tb00309.x.
Antibodies to human IgG (rheumatoid factors (RF) from serum Han resembled the 'intermediate' complexes of sera from some patients with rheumatoid arthritis. These RF were isolated from heat-inactivated serum by affinity chromatography on agarose-coupled human IgG. Indirect immunofluorescence revealed that the isolated RF cross-reacted with cell nuclei from many species. Virtually all the antinuclear factor (ANF) activity of this serum was extracted by IgG-agarose. Alternative explanations of this phenomenon, such as nonspecific binding of a separate population of ANF, binding of ANF to the immunosorbent via an IgG RF-IgG ANF immune complex, or presence of nuclear antigens on the immunosorbent, were ruled out. The cross-reacting antibodies possessed both kappa and lambda light chains and predominantly gamma and some mu heavy chains, indicating that they were of polyclonal origin. The antinuclear activity was present in the F(ab')2 fragments. The interpretation of this strange cross-reaction is briefly discussed.
人IgG抗体（来自血清Han的类风湿因子（RF））类似于一些类风湿关节炎患者血清中的“中间”复合物。这些RF通过在琼脂糖偶联的人IgG上进行亲和层析从热灭活血清中分离出来。间接免疫荧光显示，分离出的RF与许多物种的细胞核发生交叉反应。该血清中几乎所有的抗核因子（ANF）活性都被IgG琼脂糖提取出来。这种现象的其他解释，如单独一群ANF的非特异性结合、ANF通过IgG RF-IgG ANF免疫复合物与免疫吸附剂的结合或免疫吸附剂上存在核抗原，都被排除。交叉反应抗体同时具有κ和λ轻链，主要为γ和一些μ重链，表明它们是多克隆起源的。抗核活性存在于F(ab')2片段中。本文简要讨论了这种奇怪交叉反应的解释。
