Photometric or fluorometric assay of cathepsin B, L and H and papain using substrates with an aminotrifluoromethylcoumarin leaving group
- 8 January 1991
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1076 (1) , 149-151
- https://doi.org/10.1016/0167-4838(91)90232-o
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Inhibitory properties of low molecular mass cysteine proteinase inhibitors from human sarcomaBiochimica et Biophysica Acta (BBA) - General Subjects, 1989
- Cysteine‐proteinase‐inhibiting function of T kininogen and of its proteolytic fragmentsEuropean Journal of Biochemistry, 1988
- Action of Aspergillus serine proteinase on fluorogenic and chromogenic substrates.Agricultural and Biological Chemistry, 1988
- Species variations amongst lysosomal cysteine proteinasesFEBS Letters, 1984
- Sensitive fluorogenic substrates for the detection of trypsinlike proteases and pancreatic elastaseAnalytical Biochemistry, 1982
- L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and LBiochemical Journal, 1982
- [41] Cathepsin B, cathepsin H, and cathepsin LPublished by Elsevier ,1981
- Direct photometric or fluorometric assay of proteinases using substrates containing 7-amino-4-trifluoromethylcoumarinThrombosis Research, 1980
- Sensitive substrates for human leukocyte and porcine pancreatic elastase: A study of the merits of various chromophoric and fluorogenic leaving groups in assays for serine proteasesAnalytical Biochemistry, 1979
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971