Journal
CURRENT PROTEIN & PEPTIDE SCIENCE
Volume 4, Issue 3, Pages 231-251Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/1389203033487180
Keywords
aprotinin; bovine basic pancreatic trypsin inhibitor; Kunitz inhibitor; trypsin-kallikrein inhibitor; structure; inhibition properties; bio-medical aspects
Categories
Ask authors/readers for more resources
The pancreatic Kunitz inhibitor, also known as aprotinin, bovine basic pancreatic trypsin inhibitor and trypsin-kallikrein inhibitor, is one of the most extensively studied globular proteins. It has proved to be a particularly attractive and powerful toot 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available