The alkaline pH dependence of chymotrypsin reactions: postulation of a pH-dependent intramolecular competitive inhibition.
- 1 September 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 56 (3) , 833-839
- https://doi.org/10.1073/pnas.56.3.833
Abstract
The inactivity of chymotrypsinogen may be related to the intramolecular competitive inhibition described here. In the zymogen, the intramolecular competitive inhibitor would presumably be the elements of the dipeptide later removed rather than the N-terminal isoleucine or other group in the free enzyme, but the principle may be the same.This publication has 7 references indexed in Scilit:
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- Interaction of Aromatic Compounds With α-Chymotrypsin*Biochemistry, 1963
- The Effect of Aprotic Dipolar Organic Solvents on the Kinetics of α-Chymotrypsin-Catalyzed Hydrolyses*Biochemistry, 1963
- Structural changes in the activation of chymotrypsinogen and trypsinogen. Effect of urea on chymotrypsinogen and delta-chymotrypsinArchives of Biochemistry and Biophysics, 1956
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