Abstract
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).
| Original language | English |
|---|---|
| Pages (from-to) | 177-180 |
| Number of pages | 4 |
| Journal | Advances in the Biosciences |
| Volume | 65 |
| Issue number | C |
| Publication status | Published - 1987 |
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Keywords
- (pro)enzyme:inhibitor complexes
- enthalpy-entropy compensation phenomena
- macromolecular inhibitors
- Serine (pro)enzymes
- thermodynamics
Cite this
Amiconi, G., Ascenzi, P., Bolognese, M., Guarneri, M., & Menegatti, E. (1987). Enthalpy-entropy compensation phenomena in serine (Pro) enzyme: Inhibitor complex formation. Advances in the Biosciences, 65(C), 177-180.