Determination of dissociation constants of crystalline α-chymotrypsin complexes
- 5 January 1974
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 82 (1) , 27-33
- https://doi.org/10.1016/0022-2836(74)90572-5
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- X-Ray Diffraction Studies of EnzymesAnnual Review of Biochemistry, 1970
- I. Serine proteinases. The structure of α-chymotrypsinPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific SubstratesPublished by Elsevier ,1967
- Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific SubstratesJournal of Biological Chemistry, 1967
- On the interaction of the active site of α-chymotrypsin with chromophores: Proflavin binding and enzyme conformation during catalysisJournal of Molecular Biology, 1966
- The Activity of an Enzyme in the Crystalline State: Ribonuclease SJournal of Biological Chemistry, 1963
- A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counterAnalytical Biochemistry, 1960
- ACYLATION OF THE ENZYMATIC SITE OF δ-CHYMOTRYPSIN BY ESTERS, ACID ANHYDRIDES, AND ACID CHLORIDESPublished by Elsevier ,1957
- Re-evaluation of the Kinetic Constants of Previously Investigated Specific Substrates of α-Chymotrypsin1Journal of the American Chemical Society, 1955
- The reaction of p-nitrophenyl esters with chymotrypsin and insulinBiochemical Journal, 1954