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trypsin
(redirected from trypsin-like immunoreactivity (TLI))

   Also found in: Dictionary/thesaurus, Encyclopedia, Wikipedia, Hutchinson 0.01 sec.
trypsin /tryp·sin/ (trip´sin) an enzyme of the hydrolase class, secreted as trypsinogen by the pancreas and converted to the active form in the small intestine, that catalyzes the cleavage of peptide linkages involving the carboxyl group of either lysine or arginine; a purified preparation derived from ox pancreas is used for its proteolytic effect in débridement and in the treatment of empyema.tryp´tic
tryp·sin (trpsn)
n.
An enzyme of pancreatic juice that hydrolyzes proteins into smaller polypeptide units.

trypsin
[trip′sin]
Etymology: Gk, tripsis, rubbing
a proteolytic digestive enzyme produced by the exocrine pancreas that catalyzes in the small intestine the breakdown of dietary proteins to peptones, peptides, and amino acids.

trypsin, crystallized,
a proteolytic enzyme from the pancreas of the ox, Bos taurus, that has been used as a debriding agent for open wounds and ulcers.

trypsin (tripˑ·sin),
n digestive enzyme found in the stomach that breaks down protein. Also called
proteolytic enzyme, or
proteinase.

trypsin (trip´sin),
n a proteolytic digestive enzyme produced by the exocrine pancreas that catalyzes in the small intestine the breakdown of dietary proteins to peptones, peptides, and amino acids.

trypsin
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).
trypsin inhibitor
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.


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