Kinetic studies on the mechanism and the specificity of peptide semisynthesis catalyzed by the serine proteases α-chymotrypsin and β-trypsin
- 1 April 1984
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 120 (2), 686-691
- https://doi.org/10.1016/0006-291x(84)91310-x
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Use of enzymes in peptide synthesisApplied Biochemistry and Biotechnology, 1982
- Kinetic Investigation of the a‐Chymotrypsin‐Catalyzed Hydrolysis of Peptide SubstratesEuropean Journal of Biochemistry, 1982
- Resolution in high-performance liquid affinity chromatography : Dependence on eluite diffusion into the stationary phaseJournal of Chromatography A, 1981
- SHORT COMMUNICATIONHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1981
- Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. Stereochemical interpretationBiochemistry, 1973
- Binding sites for substrate leaving groups and added nucleophiles in papain-catalyzed hydrolysesBiochemistry, 1969
- Compétition nucléophile dans les réactions d'hydrolyse enzymatiqueEuropean Journal of Biochemistry, 1967
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967
- The Preparation and Properties of trans-Cinnamoyl-Papain1Journal of the American Chemical Society, 1966
- The reaction of p-nitrophenyl esters with chymotrypsin and insulinBiochemical Journal, 1954