The action of elastase on p-nitroanilide substrates
Authors:
- Joseph BiethJBJoseph Bieth
- Camille G. WermuthCWCamille G. Wermuth
- 1 July 1973
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 53 (2) , 383-390
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- N-acetyl-(L-Ala)3-p-nitroanilide as a new chromogenic substrate for elastaseBiochemical and Biophysical Research Communications, 1973
- Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substratesBiochemistry, 1973
- On the active site of elastase: Partial mapping by means of specific peptide substratesFEBS Letters, 1970
- [7] Elastase1970
- Evidence that the activity of elastase is not dependent on the ionization of its N-terminal amino groupBiochemical and Biophysical Research Communications, 1969
- Elastase-catalyzed hydrolysis of p-nitrophenyl trimethylacetateJournal of the American Chemical Society, 1968
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967
- Mechanism of Action of Proteolytic EnzymesAnnual Review of Biochemistry, 1965
- The preparation and properties of two new chromogenic substrates of trypsinArchives of Biochemistry and Biophysics, 1961
- THE INHIBITION OF CHOLINESTERASE BY PHYSOSTIGMINE AND PROSTIGMINEJournal of Biological Chemistry, 1942