Gunja-Smith Z, Nagase H, Woessner J F
Department of Medicine, University of Miami School of Medicine, FL 33101.
Biochem J. 1989 Feb 15;258(1):115-9. doi: 10.1042/bj2580115.
The 'neutral' proteoglycan-degrading metalloproteinase of human articular cartilage was purified 3,500-fold by use of an anti-(matrix metalloproteinase-3) immunoglobulin G affinity column. Molecular masses of the latent and multiple active forms and specificity of action on casein, transferrin, gelatin and fibronectin were identical with those of authentic stromelysin (matrix metalloproteinase-3) from cultured human rheumatoid synovial fibroblasts. The optimum pH of this proteinase on proteoglycan monomer was pH 5.5, and on Azocoll, 6.2; digestion of fibronectin and gelatin was more extensive at pH 5.5 than at 7.5.
利用抗(基质金属蛋白酶-3)免疫球蛋白G亲和柱,将人关节软骨的“中性”蛋白聚糖降解金属蛋白酶纯化了3500倍。其潜在形式和多种活性形式的分子量以及对酪蛋白、转铁蛋白、明胶和纤连蛋白的作用特异性,与培养的人类风湿性滑膜成纤维细胞中的正宗基质溶解素(基质金属蛋白酶-3)相同。该蛋白酶作用于蛋白聚糖单体的最适pH为5.5,作用于偶氮胶原的最适pH为6.2;在pH 5.5时对纤连蛋白和明胶的消化比在pH 7.5时更广泛。