AN INTERPRETATION OF THE KINETIC BEHAVIOR OF MODEL SUBSTRATES OF -CHYMOTRYPSIN
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Cited by 104 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. Koshland’s model as a method for the analysis of enzymatic deracemization reactions;Reports of the National Academy of Sciences of Ukraine;2021-02
2. A proposal for a three-dimensional representation of the S1 subsite of α-chymotrypsin;Bioorganic & Medicinal Chemistry Letters;1993-06
3. Studies in Bile Salt Solutions. XIV. Electronic, Charge and Steric Substrate-Effects on the Esterase Activity of Bile-Salt-Stimulated Human Milk Lipase. Hydrolysis of 4-Substituted Phenyl Propionates;Australian Journal of Chemistry;1986
4. Dynamics of ligand binding to .alpha.-chymotrypsin and to N-methyl-.alpha.-chymotrypsin;Biochemistry;1982-09-14
5. Physicochemical Property Modification Strategies Based on Enzyme Substrate Specificities II: α‐Chymotrypsin Hydrolysis of Aspirin Derivatives;Journal of Pharmaceutical Sciences;1981-12
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