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从人关节软骨组织中纯化中性蛋白聚糖降解金属蛋白酶并鉴定其为基质溶解素基质金属蛋白酶-3。

Purification of the neutral proteoglycan-degrading metalloproteinase from human articular cartilage tissue and its identification as stromelysin matrix metalloproteinase-3.

作者信息

Gunja-Smith Z, Nagase H, Woessner J F

机构信息

Department of Medicine, University of Miami School of Medicine, FL 33101.

出版信息

Biochem J. 1989 Feb 15;258(1):115-9. doi: 10.1042/bj2580115.

Abstract

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.

摘要

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。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ba64/1138331/b52737ae318b/biochemj00213-0120-a.jpg

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