Kinetic Investigation of the alpha-Chymotrypsin-Catalyzed Hydrolysis of Peptide-Ester Substrates. The Relationship between the Structure of the Peptide Moiety and Reactivity
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1975.tb02361.x/fullpdf
Reference22 articles.
1. Substrate binding site in bovine chymotrypsin Aγ. Crystallographic study using peptide chloromethyl ketones as site-specific inhibitors
2. Kinetic investigation of the crystallographically deduced binding subsites of bovine chymotrypsin Aγ
3. Kinetic Investigation of the alpha-Chymotrypsin-Catalyzed Hydrolysis of Peptide Substrates. The Relationship between Peptide-Structure N-Terminal to the Cleaved Bond and Reactivity
4. Inhibition of chymotrypsin A.alpha. with N-acyl- and N-peptidyl-2-phenylethylamines. Subsite binding free energies
5. A Numerical Method for Acquisition and Processing of Steady-State Kinetic Data Contained in an Entire Progression Curve. Application to the Study of alpha-Chymotrypsin-Catalyzed Hydrolysis
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1. Assessment of the Proteolytic Activity of α-Chymotrypsin Immobilized on Colloidal Particles by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry;Analytical Letters;2014-12
2. Simplicity within the complexity: Bilateral impact of DMSO on the functional and unfolding patterns of α-chymotrypsin;Biophysical Chemistry;2013-05
3. Chymotrypsin-catalyzed peptide synthesis;International Journal of Peptide and Protein Research;2009-01-12
4. The specificity of chymotrypsin. A statistical analysis of hydrolysis data;European Journal of Biochemistry;1991-08
5. Esterification of n-protected-tyrosine by alpha-chymotrypsin in a high concentration of ethanol;Biotechnology Techniques;1991
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