Reaction heat variation with pH in formation of the trypsin-soybean inhibitor complex.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. Potentiometric Measurement of Protein-Protein Association Constants. Soybean Trypsin Inhibitor-Trypsin Association*
2. Calorimetry of Some Trypsin-Trypsin Inhibitor Reactions
3. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
4. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution
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1. Measurement of Biochemical Affinities with a Gill Titration Calorimeter;Analytical Biochemistry;1997-12
2. Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase 1 1Edited by P. E. Wright;Journal of Molecular Biology;1997-05
3. Calorimetric study of the thermal unfolding of Kunitz-type soybean trypsin inhibitor at pH 7.0;Thermochimica Acta;1995-11
4. Calorimetric studies of the binding of Streptomyces subtilisin inhibitor to subtilisin of Bacillus subtilis strain N';Biochemistry;1985-01-15
5. A calorimetric comparison of trypsin and its anhydro modification in complex formation with Kunitz soybean inhibitor.;Journal of Biological Chemistry;1980-10
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