Conformation and Activity of Chymotrypsin: The p H-Dependent, Substrate-Induced Proton Uptake
- 19 July 1968
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 161 (3838) , 274-276
- https://doi.org/10.1126/science.161.3838.274
Abstract
Hydrogen ion uptake by chymotrypsin during reversible binding of specific substrate is shown to be due to an ionizing group of the enzyme with a pK(apparent) ∼9 in the free enzyme. This pK(apparent) is shifted to higher value in the enzyme-substrate complexes. Previous results indicating an equilibrium, controlled by this ionizing group, between active and inactive conformational forms of chymotrypsin are confirmed.Keywords
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