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

2003; Bentham Science Publishers; Volume: 4; Issue: 3 Linguagem: Inglês

10.2174/1389203033487180

1875-5550

Paolo Ascenzi, Alessio Bocedi, Martino Bolognesi, Andrea Spallarossa, Massimo Coletta, Raimondo De Cristofaro, Enea Menegatti,

Trypanosoma species research and implications

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.