Newkirk M M, Rauch J
Department of Medicine, McGill University, Montreal General Hospital Research Institute, PQ, Canada.
J Rheumatol. 1993 May;20(5):776-80.
The precise nature of the epitope on the Fc portion of the IgG molecule to which IgG rheumatoid factors (RF) bind has not been identified. As patients with rheumatoid arthritis (RA) have abnormal glycosylation of the Fc portion of IgG, we investigated the impact of the sugar present in the Fc on the binding of IgG RF.
Binding of monoclonal IgG RF to Fc fragments with varying oligosaccharide chains was detected using an immunoblot assay.
We demonstrated that the binding of human hybridoma derived monoclonal IgG RF was strongly influenced by the presence of carbohydrate and was maximal when the carbohydrate molecule was intact. The RF did not bind directly to the carbohydrate moiety itself.
This suggests that conformational changes in the polypeptide chain induced by the carbohydrate are responsible for the observed binding patterns.
尚未确定IgG类风湿因子（RF）所结合的IgG分子Fc部分表位的确切性质。由于类风湿关节炎（RA）患者的IgG Fc部分存在糖基化异常，我们研究了Fc中存在的糖对IgG RF结合的影响。
使用免疫印迹法检测单克隆IgG RF与具有不同寡糖链的Fc片段的结合。
我们证明，人杂交瘤衍生的单克隆IgG RF的结合受碳水化合物的存在强烈影响，当碳水化合物分子完整时结合最强。RF并不直接与碳水化合物部分本身结合。
这表明碳水化合物诱导的多肽链构象变化是观察到的结合模式的原因。
