Tanimoto K, Moritoh T, Azuma T, Horiuchi Y
Ann Rheum Dis. 1976 Jun;35(3):240-5. doi: 10.1136/ard.35.3.240.
Concanavalin A (Con A) froms precipitates with carbohydrate-rich protein such as IgM, IgD, IgE, and IgA. Since IgG contains little carbohydrate and does not react with Con A, the activity of IgG-rheumatoid factor (RF) can be measured in the supernate of the Con A-treated serum. When the latex fixation test (LFT) and the sensitized sheep cell agglutination test (SSCA) were perfromed in the supernate for the detection of IgG-RF, LFT was positive in 32-1% of sera, out of 137 sera originally positive for LFT, and SSCA was positive in 18-5% of sera, out of 119 sera originally positive for SSCA. IgG-RF exhibited lower complement fixing ability than IgM-RF and correlated with agglutination titres of IgG-RF, while the CH50 of the original serum did not correlate with haemolytic activities of either IgM-RF or IgG-RF.
伴刀豆球蛋白A(Con A)可与富含碳水化合物的蛋白质如IgM、IgD、IgE和IgA形成沉淀。由于IgG含碳水化合物较少且不与Con A反应,因此可在Con A处理的血清上清液中检测IgG类风湿因子(RF)的活性。当在上清液中进行乳胶凝集试验(LFT)和致敏绵羊细胞凝集试验(SSCA)以检测IgG-RF时,在最初LFT呈阳性的137份血清中,32.1%的血清LFT呈阳性,在最初SSCA呈阳性的119份血清中,18.5%的血清SSCA呈阳性。IgG-RF的补体固定能力低于IgM-RF,且与IgG-RF的凝集滴度相关,而原始血清的CH50与IgM-RF或IgG-RF的溶血活性均不相关。