An exploration of the primary specificity site of cathepsin B
- 1 April 1983
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 222 (2) , 424-429
- https://doi.org/10.1016/0003-9861(83)90540-4
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Rapid inactivation of cathepsin L by Z-Phe-PheCHN2 and Z-Phe-AlaCHN2Biochemical and Biophysical Research Communications, 1981
- Primary structure study of rat liver cathepsin B -----A striking resemblance to papainBiochemical and Biophysical Research Communications, 1980
- Degradation of fructose-1,6-bisphosphate aldolase by cathepsin BBiochemical Journal, 1980
- The hydrolysis of N-benzoyl-l-phenylalanyl-l-valyl-l-arginine-p-nitroanilide and its use as a substrate for the assay of cathepsin BAnalytical Biochemistry, 1980
- A comparison of the behavior of chymotrypsin and cathepsin B towards peptidyl diazomethyl ketonesBiochemical and Biophysical Research Communications, 1979
- Synthesis of peptides of arginine chloromethyl ketone. Selective inactivation of human plasma kallikreinBiochemistry, 1978
- The specificity of cathepsin B. Hydrolysis of glucagon at the C-terminus by a peptidyldipeptidase mechanismBiochemical Journal, 1978
- Inactivation of cathepsin B1 by diazomethyl ketonesBiochemical and Biophysical Research Communications, 1977
- Diazomethyl ketone substrate derivatives as active-site-directed inhibitors of thiol proteases. PapainBiochemistry, 1977
- Cathepsin LEuropean Journal of Biochemistry, 1977