Thermodynamics concerning the interaction of the bovine basic pancreatic trypsin inhibitor as well as bovine and porcine pancreatic secretory trypsin inhibitor with some serine (pro)enzymes has been obtained at pH 8.0 (I = 0.1 M) between 5 °C and 45 °C. Results have been analyzed by the enthalpy-entropy compensation plot (ΔHo ° versus ΔSo) and linear relationships obtained, suggesting the involvment of protein conformation and possibly hydration in the process(es) of protein-protein interaction(s).
|Number of pages||4|
|Journal||Advances in the Biosciences|
|Publication status||Published - 1987|
- (pro)enzyme:inhibitor complexes
- enthalpy-entropy compensation phenomena
- macromolecular inhibitors
- Serine (pro)enzymes