Kirk A P, O'Hara B P, Mageed R A, McMahon M S, McCarthy D, Menashi S, Archer J R, Currey H L
Clin Exp Immunol. 1986 Sep;65(3):671-8.
It has previously been shown that extracts of human articular cartilage, many many of which contain type II collagen, react with heat-aggregated immunoglobulin and artificially prepared immune complexes. Sera from patients with rheumatoid arthritis and psoriatic arthritis, but not from patients with inflammatory bowel disease, react with these extracts. There are two distinct patterns of binding, either as low molecular weight immune complexes or as free antibody directed against collagen. Aggregate-binding activity identified in extracts of human articular cartilage following pepsin digestion was found to be distinct from collagen in its salt solubility. Further purification of this aggregate-binding factor by SDS gel electrophoresis has shown it to be an artefact resulting from the binding of small immune complexes to pepsinogen present in the pepsin preparation used to digest the cartilage.
先前的研究表明，许多人关节软骨提取物含有II型胶原蛋白，它们能与热聚集免疫球蛋白及人工制备的免疫复合物发生反应。类风湿性关节炎和银屑病关节炎患者的血清能与这些提取物发生反应，而炎症性肠病患者的血清则不能。存在两种不同的结合模式，即作为低分子量免疫复合物或针对胶原蛋白的游离抗体。在胃蛋白酶消化后的人关节软骨提取物中鉴定出的聚集物结合活性，其盐溶解度与胶原蛋白不同。通过SDS凝胶电泳对这种聚集物结合因子进行进一步纯化，结果表明它是一种假象，是由于用于消化软骨的胃蛋白酶制剂中存在的小免疫复合物与胃蛋白酶原结合所致。
