Identification of the ionising group controlling the active conformation of δ-chymotrypsin in alkaline pH
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Kinetic evidence for an acyl-enzyme intermediate in the α-chymotrypsin-catalyzed hydrolysis of N-acetyl-L-tryptophan ethyl ester
2. Sigmoid and Bell-Shaped pH-Rate Profiles in α-Chymotrypsin-Catalyzed Hydrolyses. a Mechanistic Correlation
3. Amino-Acid Sequence of Bovine Chymotrypsinogen-A
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1. Acridines and Enzymes;Chemistry of Heterocyclic Compounds: A Series Of Monographs;2008-01-02
2. Structure of Crystalline α-Chymotrypsin II. A Preliminary Report Including a Hypothesis for the Activation Mechanism;Molecular Biology;1989
3. CATALYTIC GROUPS OF SERINE PROTEINASES NMR INVESTIGATIONS;Biological Applications of Magnetic Resonance;1979
4. N-Acetylbenzotriazole as a Protein Reagent. Specific Behaviour towards delta-Chymotrypsin;European Journal of Biochemistry;1976-05
5. Change in the conformation of δ-chymotrypsin upon binding a specific substrate at high pH.;FEBS Letters;1975-02-15
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