Kinetics of the reaction between trypsin and the pancreatic trypsin inhibitor
- 1 July 1957
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 66 (3) , 407-415
- https://doi.org/10.1042/bj0660407
Abstract
A potentiometric method of high sensitivity is described for following reactions in which H+ ions are liberated or absorbed. It was used to measure the extent of dissociation of the pancreatic inhibitor-trypsin compound. The kinetics of the reaction between trypsin and the pancreatic inhibitor was followed as a function of ionic strength and temperature at pH 7.8. The effects of ionic strength on the rate at 25[degree] was in accord with Bronsted-Bjerrum theory for reaction between ions of like charge, values of the net charge derived from analytical data being used. The interpretation of the heats and entropies of activation is discussed in terms of current theories of protein interaction.Keywords
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