Binding of bovine basic pancreatic trypsin inhibitor (kunitz) as well as bovine and porcine pancreatic secretory trypsin inhibitor (kazal) to human cathepsin g: A kinetic and thermodynamic study

Evandro Fioretti, Mauro Angeletti, Massimo Coletta, Paolo Ascenzi, Martino Bolognesi, Enea Menegatti, Menico Rizzi, Franca Ascoli

Research output: Contribution to journalArticlepeer-review

Abstract

The effect of pH and temperature on kinetic and thermodynamic parameters for the binding of the bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor; BPTI) as well as bovine and porcine pancreatic secretory trypsin inhibitor (Kazal inhibitor; bovine and porcine PSTI, respectively) to human cathepsin G (EC 3.4.21.20) has been investigated. The affinity of the macromolecular inhibitors examined for cathepsin G is characterized by an endothermic, entropy-driven, behaviour, and shows the following trend: BPTI

Original languageEnglish
Pages (from-to)57-64
Number of pages8
JournalJournal of Enzyme Inhibition and Medicinal Chemistry
Volume7
Issue number1
DOIs
Publication statusPublished - 1993

Keywords

  • Bovine basic pancreatic trypsin inhibitor (Kunitz)
  • Bovine pancreatic secretory trypsin inhibitor (Kazal)
  • Human cathepsin G
  • PH and temperature effects
  • Porcine pancreatic secretory trypsin inhibitor (Kazal)
  • Proteinase:inhibitor complex formation kinetics
  • Thermodynamics

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology
  • Biochemistry
  • Molecular Medicine

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