Leslie R G, Niemetz A H
Immunology. 1979 Aug;37(4):835-40.
The binding of human IgG1 and IgG3 and rabbit IgG to guinea-pig peritoneal macrophages was examined, and differences between the species, in terms of their binding mechanisms, were characterized. Rabbit IgG bound with high affinity (Kass = 3.11 +/- 0.45 x 10(6) M-1) to a finite number of receptor sites per cell (1.26 +/- 0.29 x 10(6)) and competitively inhibited the binding of guinea-pig IgG2. Heterogeneity in binding, with distinct high and low affinity components, was observed when human IgG3 was reacted with guinea-pig macrophages, while human IgG1 exhibited only low affinity binding. Neither human IgG subclass competed effectively with guinea-pig IgG2 for its cell receptor. Thus, rabbit IgG appeared to cross-react with a macrophage receptor for guinea-pig immunoglobulin, whereas the human IgG subclasses bound to macrophage membrane components that remained undefined.
研究了人IgG1和IgG3以及兔IgG与豚鼠腹腔巨噬细胞的结合情况,并对不同物种在结合机制方面的差异进行了表征。兔IgG以高亲和力(Kass = 3.11 +/- 0.45 x 10(6) M-1)结合到每个细胞有限数量的受体位点(1.26 +/- 0.29 x 10(6))上,并竞争性抑制豚鼠IgG2的结合。当人IgG3与豚鼠巨噬细胞反应时,观察到结合的异质性,具有明显的高亲和力和低亲和力成分,而人IgG1仅表现出低亲和力结合。两种人IgG亚类均不能有效地与豚鼠IgG2竞争其细胞受体。因此,兔IgG似乎与豚鼠免疫球蛋白的巨噬细胞受体发生交叉反应,而人IgG亚类则结合到尚未明确的巨噬细胞膜成分上。