STUDIES ON CATHEPSIN-B IN HUMAN ARTICULAR-CARTILAGE
STUDIES ON CATHEPSIN-B IN HUMAN ARTICULAR-CARTILAGE
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DOI：
10.1042/bj1710149
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发表时间：
1978-01-01
影响因子：
4.1
通讯作者：
YOUSUFALI, S
中科院分区：
文献类型：
--
作者：
BAYLISS, MT;YOUSUFALI, S
先前称为组织蛋白酶BI的硫醇蛋白酶组织蛋白酶B（EC 3.4.22.1）通过对合成底物的水解（Alpha.-N-benzoyl-DL-精氨酸2-萘胺）的水解在人类关节软骨中进行了测定。该酶被半胱氨酸和EDTA激活，并被碘乙酰胺和HGCL2完全抑制。整个人类血清也部分抑制了它。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，少年较高，成人和老年人的价值较低。组织蛋白酶D和组织蛋白酶B均通过软骨深度表现出区域变化。表面细胞似乎比接近软骨下骨的活性更多。
The thiol proteinase cathepsin B(EC 3.4.22.1), previously called cathepsin Bi, 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.