Evanson J M, Jeffrey J J, Krane S M
Science. 1967 Oct 27;158(3800):499-502. doi: 10.1126/science.158.3800.499.
Synovial tissue from patients with rheumatoid arthritis produces lysis of gels of reconstituted collagen fibrils in culture and releases soluble collagenase when cultured in collagen-free medium. Collagen molecules in solution at neutral pH at 20 degrees and 27 degrees C are cleaved by the synovial enzyme into (3/4) and (1/4) length fragments. In this respect the action of synovial enzyme is similar to that of amphibian collagenase and distinct from that of bacterial collagenase. At 37 degrees C reconstituted collagen fibrils and native fibers are attacked by the enzyme and further degraded to polypeptides of low molecular weight. These polypeptides are produced only after denaturation of the larger fragments, which occurs at temperatures near 37 degrees C.
类风湿性关节炎患者的滑膜组织在培养时会使重组胶原纤维凝胶发生溶解，并在无胶原培养基中培养时释放出可溶性胶原酶。在20摄氏度和27摄氏度中性pH值的溶液中的胶原分子被滑膜酶切割成(3/4)和(1/4)长度的片段。在这方面，滑膜酶的作用类似于两栖类胶原酶，与细菌胶原酶不同。在37摄氏度时，重组胶原纤维和天然纤维受到该酶的攻击，并进一步降解为低分子量的多肽。这些多肽仅在较大片段变性后产生，这种变性发生在接近37摄氏度的温度下。
