The Presence of Cathepsin B in Cartilage
- 1 January 1967
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 102 (1) , 10C-11C
- https://doi.org/10.1042/bj1020010c
Abstract
These experiments demonstrated the presence of an enzyme resembling cathepsin B in rabbit ear cartilage. Some of the properties found for cathepsin B in cartilage sections such as pH optimum, activation by cysteine and inhibition by arginine and iodoacetamide are shared by the enzyme responsible for the autolytic degradation of rabbit ear cartilage at pH 5. Further experiments are required to see whether other known synthetic substrates for cathepsins are hydrolyzed by cartilage enzymes. It should eventually be possible to show whether only cathepsin B is responsible for the autolytic release of chondromucopeptide from cartilage at pH 5 or whether it acts in conjunction with other cathepsins or enzymes.This publication has 7 references indexed in Scilit:
- A NEW SPECIFIC COLOR REACTION OF HEXURONIC ACIDSPublished by Elsevier ,2021
- The degradation of cartilage matrix by an intracellular proteaseBiochemical Journal, 1964
- Studies on the mode of action of excess of vitamin A. 6. Lysosomal protease and the degradation of cartilage matrixBiochemical Journal, 1963
- An Inhibitor of Liver Alcohol Dehydrogenase in Preparations of Reduced Diphosphopyridine NucleotideNature, 1961
- Studies on the mode of action of excess of vitamin A. 3. Release of a bound protease by the action of vitamin ABiochemical Journal, 1961
- Studies on the mode of action of excess of vitamin A. 2. A possible role of intracellular proteases in the degradation of cartilage matrixBiochemical Journal, 1961
- Studies on the mode of action of excess of vitamin A. 1. Effect of excess of vitamin A on the metabolism and composition of embryonic chick-limb cartilage grown in organ cultureBiochemical Journal, 1961