A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses
- 1 May 1991
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 275 (3) , 751-757
- https://doi.org/10.1042/bj2750751
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papainBiochemistry, 1990
- Interaction of lysosomal cysteine proteinases with α2-macroglobulin: Conclusive evidence for the endopeptidase activities of cathepsins B and HArchives of Biochemistry and Biophysics, 1989
- Analysis of kinetic data for irreversible enzyme inhibitionBiochemical Journal, 1989
- Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidinBiochimie, 1988
- Purification of cathepsin B by a new form of affinity chromatographyBiochemical Journal, 1986
- Thiol proteasesJournal of Molecular Biology, 1985
- [41] Cathepsin B, cathepsin H, and cathepsin LPublished by Elsevier ,1981
- Degradation of fructose-1,6-bisphosphate aldolase by cathepsin BBiochemical Journal, 1980
- Mapping the active site of papain with the aid of peptide substrates and inhibitorsPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959