Nelson J L, Nardella F A, Mannik M
J Immunol. 1985 Oct;135(4):2357-61.
Many idiotypic determinants on antibody molecules are thought to be located at the antigen binding site, and therefore the interaction between idiotype (Id) and anti-idiotype (anti-Id) is expected to be inhibited by the antigen. We describe two IgG and one IgM rheumatoid factors whose interactions with their respective anti-Id could only be partially inhibited by very large amounts of antigen, i.e., normal IgG. The anti-Id, however, readily inhibited the binding of their respective rheumatoid factors to IgG. The differences in interaction energies resulted in failure of antigen to readily block the Id-anti-Id interaction, and did not mean that the Id was not at the antigen combining site. The association constants for the Id-anti-Id interactions varied from 1.3 to 14.8 X 10(7) M-1, whereas the strength of the rheumatoid factor antigen bond is on the order of 10(5) M-1 for interaction with monomeric IgG. In addition, the anti-Id were able to remove rheumatoid factors that were bound to solid phase IgG, indicating that anti-Id have the potential for disrupting the immune complexes formed by antigen and antibody.
许多抗体分子上的独特型决定簇被认为位于抗原结合位点，因此独特型（Id）与抗独特型（抗Id）之间的相互作用预计会被抗原抑制。我们描述了两种IgG类风湿因子和一种IgM类风湿因子，它们与各自抗Id的相互作用仅能被极大量的抗原（即正常IgG）部分抑制。然而，抗Id能轻易抑制各自类风湿因子与IgG的结合。相互作用能量的差异导致抗原无法轻易阻断Id - 抗Id相互作用，但这并不意味着Id不在抗原结合位点。Id - 抗Id相互作用的结合常数在1.3至14.8×10⁷ M⁻¹之间，而类风湿因子与单体IgG相互作用时，其与抗原的结合强度约为10⁵ M⁻¹。此外，抗Id能够去除结合在固相IgG上的类风湿因子，这表明抗Id有破坏由抗原和抗体形成的免疫复合物的潜力。
