Baumal R, Broder I
Clin Exp Immunol. 1968 Jul;3(6):555-69.
We have found that a histamine-releasing agent, designated the rheumatoid biologically active factor (RBAF), was commonly detected in the Sephadex excluded fraction of serum and of synovial fluid obtained from patients with rheumatoid arthritis. A similar agent was also found in anaphylactoid purpura and in systemic lupus erythematosus, but not in patients with a variety of other diseases or in healthy persons. The RBAF closely resembled a soluble antigen–antibody complex, since it sedimented as a high molecular weight material and yet was specifically precipitated by goat anti-human γG-globulin. Also, the RBAF was insoluble at 50% saturation with ammonium sulphate, was stable to reduction and alkylation, underwent partial dissociation following gel filtration on Sephadex G-200 at pH 3·0, and did not stimulate the guinea-pig ileum. Moreover, the histamine-releasing activity of the RBAF was completely inhibited by human and rabbit γ-globulin. These features enabled the RBAF to be distinguished from human aggregated γ-globulin, from antibody to γ-globulin, and from anaphylatoxin, each of which also stimulated histamine release from the guinea-pig lung. The RBAF was shown to be different from both the the rheumatoid latex agglutinating factor and from the acid-dissociable γ-globulin aggregates present in the serum of some patients with rheumatoid arthritis.
我们发现，一种组胺释放因子，命名为类风湿生物活性因子（RBAF），在类风湿性关节炎患者的血清和滑液的葡聚糖凝胶排阻级分中普遍可检测到。在过敏性紫癜和系统性红斑狼疮患者中也发现了类似的因子，但在患有多种其他疾病的患者或健康人中未发现。RBAF与可溶性抗原 - 抗体复合物非常相似，因为它以高分子量物质形式沉淀，但能被山羊抗人γG球蛋白特异性沉淀。此外，RBAF在硫酸铵50％饱和度下不溶，对还原和烷基化稳定，在pH 3.0条件下在葡聚糖凝胶G - 200上进行凝胶过滤后发生部分解离，并且不刺激豚鼠回肠。此外，RBAF的组胺释放活性被人和兔γ球蛋白完全抑制。这些特性使RBAF能够与人类聚集γ球蛋白、γ球蛋白抗体以及过敏毒素区分开来，后三者也能刺激豚鼠肺释放组胺。结果表明，RBAF既不同于类风湿乳胶凝集因子，也不同于一些类风湿性关节炎患者血清中存在的酸可解离γ球蛋白聚集体。
