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 ?
Activities of amylase, trypsin and lipase in the pancreas and small intestine of the laying hen during egg formation.
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.
Such differences in the specific activity of trypsin between animals fed the two different types of diets might be attributed to their inherently different composition in terms of the molecular size of peptidic compounds rather than the dietary protein level.
The results of in-vitro trypsin degradation at different time intervals are presented in Fig.
Cyanide content, tannin content, oxalate content, trypsin inhibitor activity and haemagglutanin activity of oil seeds under study are given in Table 1.
For determine of trypsin inhibitor activity [DELTA]A / min was measured by the spectrophotometer at time drive and detection of 410 nm.
For this reason, identification of novel trypsin inhibitors is important and transgenic plants expressing these protease inhibitors have also been tested for enhanced defensive properties against insect pests (Hilder and Boulter, 1999; Franco et al.
With the criterion (pH [less than or equal to] 6, pepsins [greater than or equal to] 100 microgram/ml, trypsin [less than or equal to] 30 microgram/ml) used for predicting gastric placement 91.
Tendons frozen at -70[degrees]C and then acellularized by Trypsin 0.
The soyabean seeds were pre-heated to remove trypsin which is a proven protein inhibitor in soyabean (Friedman et al.