6-Aminoquinoline as a fluorogenic leaving group in peptide cleavage reactions: A new fluorogenic substrate for chymotrypsin
- 1 September 1981
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 116 (2) , 408-413
- https://doi.org/10.1016/0003-2697(81)90381-x
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- The preparation and properties of two new chromogenic substrates of trypsinPublished by Elsevier ,2004
- 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
- A new fluorogenic substrate for chymotrypsinAnalytical Biochemistry, 1976
- Synthetic chromogenic substrates for determination of trypsin, thrombin and thrombin-like enzymesThrombosis Research, 1972
- Spectrophotometric determination of the second dissociation constants of the aminoquinolinesJournal of Heterocyclic Chemistry, 1970
- The action of chymotrypsin on two new chromogenic substratesArchives of Biochemistry and Biophysics, 1966
- The Utilization of a Specific Chromogenic Inactivator in an “All or None” Assay for Chymotrypsin*Biochemistry, 1964
- N,N'-Carbonyldiimidazole in Peptide Synthesis. III.1 A Synthesis of Isoleucine-5 Angiotensin II Amide-IThe Journal of Organic Chemistry, 1962
- N,N'-Carbonyldiimidazole, a New Peptide Forming Reagent1Journal of the American Chemical Society, 1960
- N,N'-CARBONYLDIIMIDAZOLE, A NEW REAGENT FOR PEPTIDE SYNTHESISJournal of the American Chemical Society, 1958