The N-α-l-isoleucyl-l-valine (Ile-Val) activating dipeptide, sequentially homologous to the Ile 16-Val 17 N-terminus of bovine β-trypsin, displays an activating effect on equilibria involved in the binding of strong ligands (i.e., n-butylamine and the porcine pancreatic secretory trypsin inhibitor (Kazal-type inhibitor, type I; PSTI)) to bovine trypsinogen. This property has been investigated between pH 3.0 and 9.0 (I = 0.1 M at 21.0°C. The thermodynamics for the interaction of strong ligands with bovine β-trypsin has also been studied under the same experimental conditions. The equilibria involved in the binding of the Ile-Val activating dipeptide and/or inhibitors to bovine β-trypsin and its zymogen are described according to linkage relationships, wherefore interaction(s) between different functional and structural domains of the (pro)enzyme (i.e., the so-called Ile-Val pocket and the primary and/or secondary recognition subsite(s)), possibly revolved in the bovine trypsinogen-to-β-trypsin activation pathway, are considered.
- (Bovine pancreas)
- Enzyme activation
- Enzyme inhibitor
- Isoleucyl-l-valine activating dipeptide, N-α-l-
ASJC Scopus subject areas
- Physical and Theoretical Chemistry