The thiol proteinase cathepsin B (EC 18.104.22.168), 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.
Research Article| April 01 1978
Studies on cathepsin B in human articular cartilage
Biochem J (1978) 171 (1): 149-154.
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
M T Bayliss, S Y Ali; Studies on cathepsin B in human articular cartilage. Biochem J 1 April 1978; 171 (1): 149–154. doi: https://doi.org/10.1042/bj1710149
Download citation file: