ORIGIN OF SPECIFICITY OF ANTIGEN-ANTIBODY INTERACTION

本节的研究使我们得出这样的假设： 蛋白质结构的一个区域的状态将与 那些遥远地区产生额外的稳定能量。 从而 研究抗原结合的强度是否与 通过这种方法减少抗体远端区域的波动， 偶联，我们已经建立了5株杂交瘤细胞系，4.74.6，4.128.6， 4.145.10、2.96.12和2.34.19，产生针对 酵母异-1-细胞色素c。 单克隆IgG 1 4.74.6、4.128.6或4.145.10 与酵母细胞色素c反应，但不与克鲁斯假丝酵母细胞色素c反应， 金枪鱼、鸡、鸽子、大鼠、绵羊、狗、猪、牛或马。 单克隆IgG 1 2.96.12或2.34.19与酵母和C.克柔 细胞色素角 前者IgG 1，而不是后者也与金枪鱼反应， 兔和鸡的细胞色素C在较小程度上。 这五个人 单克隆抗体与测试的脱辅基细胞色素C反应（酵母，C. krusei和马）。 单克隆IgG 1 4.74.6、4.128.6或4.145.10不 与酵母细胞色素c的血红素或脱辅基片段反应，但不与 酵母细胞色素c的生产性片段复合物或甚至与 含有马血红素片段和酵母脱辅基细胞色素的杂合复合物 C. 根据杂交复合物的试验，抗原决定簇 对于这三种抗体，其似乎位于残基59至108。 单克隆IgG 1 2.96.12和2.34.19不与任何这些反应 复合物或杂化复合物。 结果表明，所有这五个 单克隆抗体识别的三维结构的 由天然细胞色素c折叠形成的抗原决定簇（和 前三种情况下的复合物）。 此外，三 以前的抗体更特异地识别氨基的侧链， 两个人在一起，比在一起的时间更长。 然而，后两者 抗体区分天然蛋白质和片段复合物 但前三种都没有。

The studies in this Section have led us to the hypothesis that the energy state of one region of the structure of proteins would be coupled with those of distant regions to generate extra stabilizing energy. Thus, to investigate whether the strength of antigen binding is related to the reduction of the fluctuation of distant regions of the antibody by such coupling, we have developed 5 hybridoma cell lines, 4.74.6, 4.128.6, 4.145.10, 2.96.12 and 2.34.19 producing monoclonal IgG1 directed against yeast iso-1-cytochrome c. Monoclonal IgG1 4.74.6, 4.128.6 or 4.145.10 reacts with yeast cytochrome c but not with cytochrome c of Candida krusei, tuna, chicken, pigeon, rat, sheep, dog, porcine, bovine or horse. Monoclonal IgG1 2.96.12 or 2.34.19 reacts with both yeast and C. krusei cytochromes c. The former IgG1, but not the latter also reacts with tuna, rabbit and chicken cytochromes c in a lesser extent. None of these five monoclonal antibodies reacts with the apocytochromes c tested (yeast, C. krusei and horse). Monoclonal IgG1 4.74.6, 4.128.6 or 4.145.10 does not react with heme- or apofragments of yeast cytochrome c but does react with the productive fragment complexes of yeast cytochrome c or even with the hybrid complexes containing the horse heme fragment and yeast apocytochrome c. On the basis of tests with hybrid complexes, the antigenic determinants for these three antibodies appear to be located in residues 59 to 108. Monoclonal IgG1 2.96.12 and 2.34.19 do not react with any of these complexes or hybrid complexes. The results indicate that all of these five monoclonal antibodies recognize the three-dimensional configuration of the antigenic determinant formed by folding of the native cytochrome c (and also the complexes in the three former cases). In addition, the three former antibodies more specifically recognize the side chains of the amino acids in the determinant than the two latter. However, the two latter antibodies discriminate between the native protein and the fragment complex but the three former do not.