Binding rates, oxygen-sulfur substitution effects, and the pH dependence of chymotrypsin reactions
- 19 April 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (8) , 1573-1580
- https://doi.org/10.1021/bi00627a007
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 11 references indexed in Scilit:
- The Kinetics of the Two-Step Interaction of Chymotrypsin with ProflavinJournal of Biological Chemistry, 1967
- The binding of inhibitors to α-chymotrypsinBiochemical Journal, 1966
- On the interaction of the active site of α-chymotrypsin with chromophores: Proflavin binding and enzyme conformation during catalysisJournal of Molecular Biology, 1966
- Implication of an Ionizing Group in the Control of Conformation and Activity of ChymotrypsinJournal of Biological Chemistry, 1966
- The α-chymotryptic hydrolysis of glycine estersBiochemical Journal, 1966
- The Acyl-Enzyme Dimer of Chymotrypsin*Biochemistry, 1965
- The Effect of Aprotic Dipolar Organic Solvents on the Kinetics of α-Chymotrypsin-Catalyzed Hydrolyses*Biochemistry, 1963
- Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)Published by Wiley ,1963
- The Kinetics of the α-Chymotrypsin-Catalyzed Hydrolysis of p-Nitrophenyl Acetate*Biochemistry, 1962
- The effect of pH on the affinities of enzymes for substrates and inhibitorsBiochemical Journal, 1953