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chymotrypsin

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chymotrypsin /chy·mo·tryp·sin/ (ki″mo-trip´sin) an endopeptidase with action similar to that of trypsin, produced in the intestine by activation of chymotrypsinogen by trypsin; a product crystallized from an extract of the pancreas of the ox is used clinically for enzymatic zonulolysis and debridement.
chy·mo·tryp·sin (km-trpsn)
n.
A pancreatic digestive enzyme that catalyzes the hydrolysis of certain proteins in the small intestine into polypeptides and amino acids.

chymo·tryptic (-tk) adj.

chymotrypsin
[kī′mōtrip′sin]
Etymology: Gk, chymos + tryein, to rub, pepsin, digestion
1 a proteolytic enzyme produced by the pancreas that catalyzes the hydrolysis of casein and gelatin.
2 a yellow crystalline powder prepared from an extract of ox pancreas that is used in treating digestive disorders in which the enzyme is present in less than normal amounts or is totally lacking.

chymotrypsin [ki″mo-trip´sin]
1. an enzyme with action similar to that of trypsin, produced in the intestine by activation of chymotrypsinogen.
2. a preparation crystallized from an extract of the pancreas of the ox, used clinically for enzymatic dissolution of the zonular membrane of the eye.

chymotrypsin
an endopeptidase with action similar to that of trypsin, produced in the intestine by activation of chymotrypsinogen from the exocrine pancreas; a product crystallized from an extract of the pancreas of the ox has been used clinically as an anti-inflammatory agent and for enzymatic zonulolysis and débridement.

chymotrypsin test
a test of pancreatic exocrine efficiency depending on the presence of chymotrypsin to split a peptide-para-aminobenzoic acid compound.

chymotrypsin
Physiology A GI tract serine protease synthesized in the pancreas as a prohormone, which cleaves proteins at hydrophobic amino acids–leucine, phenylalanine, tryptophan, tyrosine


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He says porcine pancreas contains a complex of natural enzymes including protease, amylase, lipase, trypsin, chymotrypsin, esterase, peptidase, nuclease, clastase and collagenase, a content similar to that of human pancreatic enzymes.
From the HPLC analysis results we identified 9 different protease and chymotrypsin inhibitors in the natural samples, such as aeruginopeptin 917S-A, anabaenopeptin F, microcin SF608, micropeptin T-20, nodulapeptin B, planktopeptin BL 1061, oscillamide Y, oscillapeptilide 97-A, and oscillapeptilide 97-B (Table 2; Fig.
 
 
 
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