The Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor): A Milestone Protein

Author(s): Paolo Ascenzi, Alessio Bocedi, Martino Bolognesi, Andrea Spallarossa, Massimo Coletta, Raimondo De Cristofaro, Enea Menegatti

Journal Name: Current Protein & Peptide Science

Volume 4 , Issue 3 , 2003

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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 chymotrypsinand 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.

Keywords: aprotinin, bovine basic pancreatic trypsin inhibitor, kunitz inhibitor, trypsin-kallikrein inhibitor, structure, inhibition properties, bio-medical aspects

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Article Details

Year: 2003
Published on: 01 March, 2012
Page: [231 - 251]
Pages: 21
DOI: 10.2174/1389203033487180
Price: $65

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