关于人关节软骨中组织蛋白酶B的研究。
Studies on cathepsin B in human articular cartilage.
作者信息
Bayliss M T, Ali S Y
出版信息
Biochem J. 1978 Apr 1;171(1):149-54. doi: 10.1042/bj1710149.
Abstract
The thiol proteinase cathepsin B (EC 3.4.22.1), previously called cathepsin B1, was assayed in human articular cartilage by its hydrolysis of the synthetic substrate alpha-N-benzoyl-DL-arginine 2-naphthylamide. The enzyme was activated by cysteine and EDTA and completely inhibited by iodoacetamide and HgCl2. It was also partially inhibited by whole human serum. Human osteoarthrotic cartilage had increased activity when compared with normal cartilage. Cathepsin B activity of normal cartilage was age-related, being high in juveniles and declining to low values in adult and elderly individuals. Cathepsin D and cathepsin B both exhibited a zonal variation through the cartilage depth; the surface cells appeared to contain more activity than those close to the subchondral bone.
摘要
硫醇蛋白酶组织蛋白酶B（EC 3.4.22.1），以前称为组织蛋白酶B1，通过其对合成底物α-N-苯甲酰-DL-精氨酸2-萘酰胺的水解作用，在人关节软骨中进行测定。该酶被半胱氨酸和EDTA激活，并被碘乙酰胺和HgCl2完全抑制。它也被全人血清部分抑制。与正常软骨相比，人骨关节炎软骨的活性增加。正常软骨的组织蛋白酶B活性与年龄相关，在青少年中较高，在成年人和老年人中降至低值。组织蛋白酶D和组织蛋白酶B在软骨深度上均表现出区域差异；表面细胞似乎比靠近软骨下骨的细胞含有更多的活性。
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