Giacomello A, Salerno C, Gigante M C
Experientia. 1981 Oct 15;37(10):1070-1. doi: 10.1007/BF02085013.
The affinity between purified rheumatoid factors (RF) and native or heat aggregated human IgG has been studied in vitro by polarization fluorescence in the presence and in the absence of D-penicillamine. The value of the dissociation constant was the same using native and heat aggregated IgG suggesting that binding to the aggregated protein is not dependent on the exposure of a new determinant lacking in the native molecule. The results obtained in the presence of D-penicillamine suggest that the concentration of the drug necessary to get a pronounced effect on the apparent dissociation constant of the immunocomplex between IgG and RF is not reached in vivo, in clinical situations.
在有和没有D-青霉胺存在的情况下，通过偏振荧光体外研究了纯化的类风湿因子（RF）与天然或热聚集的人IgG之间的亲和力。使用天然和热聚集的IgG时，解离常数的值相同，这表明与聚集蛋白的结合不依赖于天然分子中不存在的新决定簇的暴露。在D-青霉胺存在下获得的结果表明，在临床情况下，体内未达到对IgG和RF之间免疫复合物的表观解离常数产生显著影响所需的药物浓度。
