The interaction of trifluoroacetyl peptide chloromethyl ketones with porcine pancreatic elastase. Direct evidence for nonproductive enzyme.inhibitor complexes.
Open Access
- 1 June 1979
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 254 (12) , 5208-5218
- https://doi.org/10.1016/s0021-9258(18)50580-9
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Fluorotyrosine alkaline phosphatase: Internal mobility of individual tyrosines and the role of chemical shift anisotropy as a 19F nuclear spin relaxation mechanism in proteinsPublished by Elsevier ,2006
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Unusual reactivity of trifluoroacetyl peptide chloromethyl ketones with pancreatic elastaseJournal of the American Chemical Society, 1978
- Trifluoroacetylated peptides as substrates and inhibitors of elastase: a nuclear magnetic resonance studyBiochemistry, 1976
- The active site of porcine elastaseJournal of Molecular Biology, 1975
- The action of elastase on p-nitroanilide substratesBiochemical and Biophysical Research Communications, 1973
- Peptide chloromethyl ketones as irreversible inhibitors of elastaseBiochemistry, 1973
- Elastase-catalyzed amide hydrolysis of triand tetrapeptide amidesBiochemistry, 1973
- Active-site specific inhibitors of elastaseJournal of the American Chemical Society, 1972
- Ethyl Thioltrifluoroacetate as an Acetylating Agent with Particular Reference to Peptide Synthesis1Journal of the American Chemical Society, 1955