Characterization of a Reversibly Formed Enzyme Complex in the Reaction of Chymotrypsin with Diisopropyl Fluorophosphate
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. Conformational Changes Accompanying An Enzyme Catalyzed Reaction
2. CONFORMATIONAL CHANGES IN ENZYME CATALYSIS
3. Evidence for Conformational Changes in α-Chymotrypsin-catalyzed Reactions. VI. Changes in Optical Rotatory Dispersion Parameters
4. Evidence for Conformational Changes in α-Chymotrypsin Catalyzed Reactions. VII. Thermal Induced Reversible Changes of Conformation at pH 2.0
5. Interpretation of the ultraviolet spectrum of trans-cinnamoyl-α-chymotrypsin
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1. Extraterritoriality of US Patent Law and 35 USC §271(g): Strategies for Increasing Protection for Patented Methods of Screening Compound Libraries;Biotechnology Law Report;2011-06
2. Conformational Adaptability in Enzymes;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. References;Laboratory Techniques in Biochemistry and Molecular Biology;1976
4. 7 Chymotrypsin-Chemical Properties and Catalysis;Hydrolysis: Peptide Bonds;1971
5. The Inhibition of Porcine Pancreas Kallikrein by Di-Isopropyl-Fluorophosphate. Kinetics, Stoichiometry, and Nature of the Group Phosphorylated;European Journal of Biochemistry;1969-10
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