Bovine trypsinogen activation. A thermodynamic study

Massimo Coletta, Paolo Ascenzi, Gino Amiconi, Martino Bolognesi, Mario Guarneri, Enea Menegatti

Research output: Contribution to journalArticle


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.

Original languageEnglish
Pages (from-to)355-362
Number of pages8
JournalBiophysical Chemistry
Issue number1-3
Publication statusPublished - Aug 31 1990


  • (Bovine pancreas)
  • Enzyme activation
  • Enzyme inhibitor
  • Isoleucyl-l-valine activating dipeptide, N-α-l-
  • Thermodynamics
  • Trypsin,β-
  • Trypsinogen

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Physical and Theoretical Chemistry

Fingerprint Dive into the research topics of 'Bovine trypsinogen activation. A thermodynamic study'. Together they form a unique fingerprint.

  • Cite this

    Coletta, M., Ascenzi, P., Amiconi, G., Bolognesi, M., Guarneri, M., & Menegatti, E. (1990). Bovine trypsinogen activation. A thermodynamic study. Biophysical Chemistry, 37(1-3), 355-362.