trypsin


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Related to trypsin: chymotrypsin

trypsin

 [trip´sin]
a proteolytic enzyme formed in the intestine by the cleavage of trypsinogen by enterokinase. It is an endopeptidase that hydrolyzes peptides of arginine or lysine.

tryp·sin

(trip'sin),
A proteolytic enzyme formed in the small intestine from trypsinogen by the action of enteropeptidase; a serine proteinase that hydrolyzes peptides, amides, esters, etc., at bonds of the carboxyl groups of l-arginyl or l-lysyl residues; it also produces the meromyosins.

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

trypsin

(trĭp′sĭn)
n.
A pancreatic enzyme that catalyzes the hydrolysis of proteins to form smaller polypeptide units.

tryp′tic (-tĭk) adj.

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.

tryp·sin

(trip'sin)
A proteolytic enzyme formed from trypsinogen in the small intestine by the action of enteropeptidase; a serine proteinase that hydrolyzes peptides, amides, and esters.

trypsin

One of the digestive enzymes secreted by the pancreas as the precursor trypsinogen, that breaks down protein to polypeptide fragments. These are then split further to amino acids by carboxypeptidase from the pancreas and aminopeptidase from the small intestine.

trypsin

an endopeptidase enzyme which breaks down PROTEIN into POLYPEPTIDES. It is secreted, as part of the PANCREATIC JUICE, in the form of an inactive precursor, trypsinogen, which is converted to trypsin by ENTEROKINASE secreted in the SMALL INTESTINE.

trypsin (tripˑ·sin),

n digestive enzyme found in the stomach that breaks down protein. Also called
proteolytic enzyme, or
proteinase.

tryp·sin

(trip'sin)
Proteolytic enzyme formed in small intestine from trypsinogen by action of enteropeptidase; serine proteinase that hydrolyzes peptides, amides, and esters, at bonds of carboxyl groups of l-arginyl or l-lysyl residues.

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.
References in periodicals archive ?
Autocrine induction of invasion and metastasis by tumor-associated trypsin inhibitor in human colon cancer cells.
2 - trypsin's concentration, mg/ml; m - dilution of inhibitor's solution; 200 - the amount of trypsin in 1 ml (200 mkg); 21 - ratio of tissue's charge to extragent, weight 100 mg.
2] subunit yields residues G-L-F-G-A-I-A-G-, indicating that the cleavage sites by tryptase Clara and trypsin are between [R.
In previous reports, only trypsin inhibitory activity was studied; however, in this work, also chymotrypsin inhibitory activity and elastase inhibitory activity are reported at least as part of the crude extract, which increases the diversity of serine protease inhibitors for Opuntia (Torres-Castillo et al.
The study showed that trypsin inhibitors in the seeds were inactivated by heat treatment; trypsin inhibitors are known to be heat-labile and can be partially or completely denatured when exposed to elevated temperature.
The chief difference between trypsin and chymotrypsin seems to be in their specificity.
The total analysis time (immunocapture, buffer exchange, trypsin digestion, de-salting and reversed phase) on the workstation was 45 min.
Keywords: Cell proliferation, Epithelial cells, Immunophenotyping, Placenta, Stem cell, Trypsin
Trypsin, chymotrypsin, and elastase activities in extracts of 5 mg total protein from larval guts of laboratory (NL, US), field (GTO), and Xentari-selected (USX) strains were compared.
Cyclo(L-Tyr-L-Pro) (diketopiperazine) and o-hydroxyemodin (anthraquinone) exhibited potent inhibitory effect on HCV NS3-NS4A protease with mild interfere with human physiological processes requiring trypsin activity, which warrants for further investigation of other members of these widely distributed class of diketopiperazines and anthraquinones in marine and terrestrial metabolites.