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

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

tryp′tic (-tĭk) adj.

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.

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.
References in periodicals archive ?
On the other hand, the low expression levels observed for the trypsin during the first days of C.
On the whole, the AMS, lipase and trypsin activities in duodenum, jejunum and ileum were the highest in the 30 h group (p<0.05), and then the 24 h group was second only to the 30 h group in terms of these three enzyme activities.
Protocols I (5 mM EDTA; 50 mM TRIS; 0.5% antibiotic) and II (5 mM EDTA + 0.05% trypsin + 0.5% antibiotic) were tested in both portions (fetal and maternal) of the placentas.
Trypsin and chymotrypsin activity assays performed in triplicate showed consistent results.
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.
Following the same methodological steps, inhibitory activity for trypsin was repeated by pre-testing the RTs of seed and flour under denaturing conditions (100 [degrees]C for 10 minutes).
Solutions of 20 mmol [l.sub.-1] N-p-tosyl-L-lys-chloromethyl ketone (TLCK; T7254; Sigma-Aldrich) in 1 mmol [l.sub.-1] HC1 and 200 mmol [l.sub.-1] phenylmethanesulphonyl fluoride (PMSF; P7626, Sigma-Aldrich) in 2-propanol to identify trypsin and serine proteinase activity, respectively.
Chromatographic separation of trypsin solution 52 [micro]mol x [L.sup.-1] (100%) and some fractional dilutions (related to 90%; 80%; 70%; 60%; 50%; 40%; 30%; 20%; 10%; 5%; and 2.5% of initial concentration) was performed.
The trypsin inhibition activity per gram of protein was highest in the nonprecipitated fraction that remained after incubation in ethanol (Table 4).
Porcine trypsin and bovine thrombin were purchased from Serva Electrophoresis GmbH (Heidelberg, Germany) and the latter was further purified as described in [10] yielding a preparation with specific activity of 2100 IU/mg.