人关节软骨的低分子量丝氨酸蛋白酶抑制剂。分离、特性鉴定及生物合成。
Low molecular weight serine proteinase inhibitors of human articular cartilage. Isolation, characterization, and biosynthesis.
作者信息
Andrews J L, Ghosh P
机构信息
Raymond Purves Research Laboratories, University of Sydney, Royal North Shore Hospital of Sydney, St. Leonards, New South Wales, Australia.
出版信息
Arthritis Rheum. 1990 Sep;33(9):1384-93. doi: 10.1002/art.1780330911.
The major low molecular weight serine proteinase inhibitor of human articular cartilage was purified to homogeneity as determined by single-peak elution with 4 high resolution techniques. The purified protein was found to be a potent inhibitor of human leukocyte elastase and cathepsin G, as well as the native serine proteinases derived from human articular cartilage and intervertebral disc. The inhibitor and lysozymes were synthesized by human articular cartilage in vitro. These properties and the ability of this cationic inhibitor to bind to cartilage matrix components suggest a possible role in the modulation of matrix catabolism in normal and pathologic states.
人类关节软骨的主要低分子量丝氨酸蛋白酶抑制剂经4种高分辨率技术单峰洗脱测定，已纯化至同质。发现纯化后的蛋白质是人类白细胞弹性蛋白酶和组织蛋白酶G的有效抑制剂，也是源自人类关节软骨和椎间盘的天然丝氨酸蛋白酶的有效抑制剂。该抑制剂和溶菌酶可由人类关节软骨在体外合成。这些特性以及这种阳离子抑制剂与软骨基质成分结合的能力表明，它在正常和病理状态下的基质分解代谢调节中可能发挥作用。
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