Nucleophile specificity in chymotrypsin peptide synthesis
- 1 January 1984
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 118 (1) , 317-323
- https://doi.org/10.1016/0006-291x(84)91103-3
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Enzyme peptide synthesis and semisynthesis: Kinetic and thermodynamic aspectsJournal of Theoretical Biology, 1982
- Synthesis of pure p-chlorophenyl-L-alanine form L-phenylalanineJournal of Medicinal Chemistry, 1974
- Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1973
- Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. Stereochemical interpretationBiochemistry, 1973
- Determination of the individual rate constants of α‐chymotrypsin‐catalyzed hydrolysis with the added nucleophilic agent, 1,4‐butanediolFEBS Letters, 1971
- Specificity of α‐chymotrypsin. Dipeptide substratesFEBS Letters, 1970
- Optical Rotation of Peptides. III. Lysine Dipeptides1Journal of the American Chemical Society, 1951
- Optical Rotation of Peptides. I. Glycine and Alanine Dipeptides1Journal of the American Chemical Society, 1951
- The Apparent Ionization Constants of Acethydrazide and GlycylhydrazideJournal of the American Chemical Society, 1949