trypsin inhibitor(redirected from Trypsin inhibitors)
1. a peptide formed from trypsinogen through hydrolysis under the catalytic influence of enteropeptidase, with trypsin also produced as a result; so called because the peptide masks or inhibits the active site of the trypsin molecule;
2. one of the polypeptides, from various sources (for example, human and bovine colostrum, soybeans, egg white), that inhibit the action of trypsin. Compare: Bowman-Birk inhibitor.
one of a group of peptides, present in such varied sources as soybeans, egg white, and human colostrum, that mask or inhibit the active site of the trypsin molecule. Also called kunitz inhibitor.
a proteolytic enzyme formed in the intestine by the cleavage of trypsinogen by enterokinase. Trypsinogen enters the intestine as part of the intestinal juice. It is an endopeptidase that hydrolyzes peptides of arginine or lysine.
trypsin fecal tests
see fecal trypsin.
feline trypsin-like immunoreactivity (fTLI)
see trypsin-like immunoreactivity (below).
small protein synthesized in the exocrine pancreas which prevents conversion of trypsinogen to trypsin, so protecting itself against trypsin digestion. Pancreatic trypsin inhibitor competitively binds to the active site of trypsin and inactivates it at a very low concentration. The binding is amongst the strongest noncovalent associations, but only a fraction of the potential trypsin is so inhibited.
trypsin-like immunoreactivity (TLI)
serum proteins, particularly trypsinogen, react immunologically as trypsin and a normal level is dependent upon a normally functional pancreas. This is used in the diagnosis of exocrine pancreatic insufficiency.