Trissl D, Kolb H
Eur J Immunol. 1975 Jan;5(1):39-43. doi: 10.1002/eji.1830050109.
Within individual sera, mouse IgG1 and IgG2a subclass antibodies against the antigenic determinant oligo-D-alanine are likely to have similar combining sites. The antibodies are characterized by two methods, by their rate of binding to antigen equipped sheep red blood cells and by the hapten inhibition of antigen binding. The two characteristics are shown to be independent. The subclass antibodies of thirteen different sera differ by a factor of about 10 in their rate constant and by a factor of about 50 in affinity for hapten. In contrast, IgG1 and IgG2a within the same serum have strikingly similar rate constants (factor 1.02-1.33) as well as very similar affinities (factor 1.1-2.7). Since it is highly improbable that correlation in two independent criteria occurs by chance, the IgG1 and IgG2a antibodies are assumed to have similar combining sites.
在个体血清中,针对抗原决定簇寡聚-D-丙氨酸的小鼠IgG1和IgG2a亚类抗体可能具有相似的结合位点。通过两种方法对抗体进行表征,即它们与抗原包被的绵羊红细胞的结合速率以及半抗原对抗原结合的抑制作用。结果表明这两个特征是相互独立的。13种不同血清的亚类抗体在速率常数上相差约10倍,对半抗原的亲和力相差约50倍。相比之下,同一血清中的IgG1和IgG2a具有非常相似的速率常数(1.02 - 1.33倍)以及非常相似的亲和力(1.1 - 2.7倍)。由于两个独立标准之间的相关性不太可能偶然出现,因此假定IgG1和IgG2a抗体具有相似的结合位点。