Determination of the binding constant of a specific ester and a specific amide substrate to α-chymotrypsin
- 17 February 1966
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 22 (4), 447-452
- https://doi.org/10.1016/0006-291x(66)90668-1
Abstract
No abstract availableFunding Information
- National Science Foundation
- National Institutes of Health
This publication has 7 references indexed in Scilit:
- Kinetics of the Reaction of α-Chymotrypsin with Diisopropyl Fluorophosphate, with Measurements of Hydrogen Ion Release, Enzyme Inhibition, and Spectral Changes of Enzyme at 290 mµPublished by Elsevier ,1965
- Mechanism of Action of Proteolytic EnzymesAnnual Review of Biochemistry, 1965
- The Anatomy of an Enzymatic Catalysis. α-ChymotrypsinJournal of the American Chemical Society, 1964
- Interaction of Aromatic Compounds With α-Chymotrypsin*Biochemistry, 1963
- Spectroscopic Studies of α-Chymotrypsin Catalyzed Reactions. II. Spectral Changes at 290 mμJournal of the American Chemical Society, 1962
- The mechanism of the reaction of chymotrypsin with p-nitrophenyl acetateBiochemical Journal, 1956
- The reaction of p-nitrophenyl esters with chymotrypsin and insulinBiochemical Journal, 1954