Thermodynamics of α-Chymotrypsin-Inhibitor Complex Formation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. Thermodynamic Study of an Enzyme—Substrate Complex of Chymotrypsin. I1,2
2. Thermodynamic Study of Some Enzyme—Inhibitor Complexes of Chymotrypsin. II1,2
3. The Interaction of Purified Antibody with Optically Isomeric Haptens1,2
4. Solvent Effects in the α-Chymotrypsin—Hydrocinnamic Ester System1
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1. Calorimetric studies on solid α-chymotrypsin preparations in air and in organic solvents;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-06
2. Solvation effects upon the thermodynamic substrate activity; correlation with the kinetics of enzyme catalyzed reactions. I. Effects of added reagents such as methanol upon alpha-chymotrypsin;Biophysical Chemistry;1992-06
3. Probing the molecular dimensions of general anaesthetic target sites in tadpoles (Xenopus laevis) and model systems using cycloalcohols;British Journal of Pharmacology;1991-01
4. A new mechanism for the terminal stages of complement hemolysis based on kinetic and thermodynamic rationales;Biochemical and Biophysical Research Communications;1982-08
5. Thermal behavior of bovine β-trypsin at physiological temperature range;Archives of Biochemistry and Biophysics;1980-10
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