Physical Evidence for the Existence of at Least Two Salt-dependent Forms of α-Chymotrypsin at Slightly Acid pH
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
1. A NMR study of the interaction of N-trifluoroacetyl-D-phenylalanine with α-chymotrypsin
2. Nuclear magnetic resonance studies of the interaction of tryptophan with .alpha.-chymotrypsin
3. Thermodynamics of α-Chymotrypsin-Substrate and Inhibitor Complex Formation as a Function of pH
4. ESR probing of macromolecules: Function and operation of structural units within the active site of α-chymotrypsin
5. Spectrophotometric and kinetic evidence for the existence of at least two salt-dependent conformations of α-chymotrypsin at pH values near neutrality
Cited by 14 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Activation and stabilization of α-chymotrypsin by cationic additives;European Journal of Biochemistry;2001-12-15
2. Solvation effects upon the thermodynamic substrate activity; correlation with the kinetics of enzyme catalyzed reactions. II. More complex interactions of alpha-chymotrypsin with dioxane and acetone which are also competitive inhibitors;Biophysical Chemistry;1992-06
3. Kinetic salting effect as a promising tool in the investigation of enzyme molecule changes upon reaction: Deacylation of acyl-chymotrypsins;Bioorganic Chemistry;1990-06
4. Structure-function relationships in the inorganic salt-induced precipitation of α-chymotrypsin;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1989-05
5. The principles of enzyme stabilization IV. Modification of ‘key’ functional groups in the tertiary structure of proteins;Biochimica et Biophysica Acta (BBA) - Enzymology;1979-03
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