The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): A milestone protein

Paolo Ascenzi, Alessio Bocedi, Martino Bolognesi, Andre Spallarossa, Massimo Colletta, Raimondo De Cristofaro, Enea Menegatti

Research output: Contribution to journalArticlepeer-review


The pancreatic Kunitz inhibitor, also known as aprotinin, bovine basic pancreatic trypsin inhibitor (BPTI) and trypsin-kallikrein inhibitor, is one of the most extensively studied globular proteins. It has proved to be a particularly attractive and powerful tool for studying protein conformation as well as molecular bases of protein/protein interaction(s) and (macro)molecular recognition. BPTI has a relatively broad specificity, inhibiting trypsin- as well as chymotrypsin- and elastase-like serine (pro)enzymes endowed with very different primary specificity. BPTI reacts rapidly with serine proteases to form stable complexes, but the enzyme:inhibitor complex formation may involve several intermediates corresponding to discrete reaction steps. Moreover, BPTI inhibits the nitric oxide synthase type-I and -II action and impairs K+ transport by Ca2+-activated K+ channels. Clinically, the use of BPTI in selected surgical interventions, such as cardiopulmonary surgery and orthotopic liver transplantation, is advised, as it significantly reduces hemorrhagic complications and thus blood-transfusion requirements. Here, the structural, inhibition, and bio-medical aspects of BPTI are reported.

Original languageEnglish
Pages (from-to)231-251
Number of pages21
JournalCurrent Protein and Peptide Science
Issue number3
Publication statusPublished - Jun 2003


  • Aprotinin
  • Bio-medical aspects
  • Bovine basic pancreatic trypsin inhibitor
  • Inhibition properties
  • Kunitz inhibitor
  • Structure
  • Trypsin-kallikrein inhibitor

ASJC Scopus subject areas

  • Biochemistry


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