Bjelle A, Osterlin S
J Rheumatol. 1976 Dec;3(4):400-8.
Cathepsin D type proteases were extracted from articular cartilage, synovial membrane, and synovial fluid from normal, adult bovine knee joints. A sensitive enzyme assay made it possible to measure protease activity in the different tissues from individual joints. Highest activity was found in the synovial membrane, while cell free synovial fluids contained comparatively low activity. The degrading effect on articular cartilage proteoglycans (PGC and PGS), isolated from the same joints, was demonstrated by gelfiltration on Sepharose columns and by viscometry. Gelfiltration profiles of incubation mixtures indicated a proteolytic effect on PGC and on PGS), at pH 3.5, in concentrations of enzyme and proteoglycans found in cartilage tissue. No effect at neutral pH was obtained despite a 100-fold increase of enzyme concentration. These findings were supported by viscometry data. The degrading effect of enzymes from all sources was completely inhibited by pepstatin.
从成年正常牛膝关节的关节软骨、滑膜和滑液中提取组织蛋白酶D型蛋白酶。一种灵敏的酶测定方法使得测量各个关节不同组织中的蛋白酶活性成为可能。滑膜中的活性最高，而无细胞滑液中的活性相对较低。通过在琼脂糖柱上进行凝胶过滤和粘度测定，证明了从相同关节分离出的蛋白酶对关节软骨蛋白聚糖（PGC和PGS）具有降解作用。孵育混合物的凝胶过滤图谱表明，在软骨组织中发现的酶和蛋白聚糖浓度下，在pH 3.5时对PGC和PGS有蛋白水解作用。尽管酶浓度增加了100倍，但在中性pH下未观察到作用。粘度测定数据支持了这些发现。所有来源的酶的降解作用均被胃蛋白酶抑制剂完全抑制。
