The binding of specific and non‐specific aldehyde substrate analogs to α‐chymotrypsin
- 1 August 1975
- journal article
- Published by Wiley in FEBS Letters
- Vol. 56 (1), 81-84
- https://doi.org/10.1016/0014-5793(75)80116-5
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- The binding of a non-specific ‘transition state analogue’ to α-chymotrypsinFEBS Letters, 1975
- Comparative study of various serine alkaline proteinases from microorganismsArchives of Biochemistry and Biophysics, 1974
- Binding of boronic acids to chymotrypsinBiochemistry, 1974
- High resolution nuclear magnetic resonance studies of the active site of chymotrypsin: II. Polarization of histidine 57 by substrate analogues and competitive inhibitorsJournal of Molecular Biology, 1974
- Transition‐state analogs of an aliphatic amidaseFEBS Letters, 1973
- Use of peptide aldehydes to generate transition-state analogs of elastaseBiochemistry, 1973
- Peptide aldehydes inhibiting chymotrypsinBiochemical and Biophysical Research Communications, 1972
- 2-Phenylethaneboronic acid, a possible transition-state analog for chymotrypsinBiochemistry, 1971
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1969
- The Mechanism of α-Chymotrypsin-catalyzed Hydrolyses1-3Journal of the American Chemical Society, 1962