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- Title
The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): a milestone protein.
- Authors
Ascenzi, Paolo; Bocedi, Alessio; Bolognesi, Martino; Spallarossa, Andrea; Coletta, Massimo; De Cristofaro, Raimondo; Menegatti, Enea
- Abstract
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.
- Publication
Current protein & peptide science, 2003, Vol 4, Issue 3, p231
- ISSN
1389-2037
- Publication type
Journal Article
- DOI
10.2174/1389203033487180