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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 A, B, or C; a serine proteinase of the gastrointestinal tract that preferentially cleaves carboxyl links of hydrophobic amino acids, particularly at tyrosyl, tryptophanyl, phenylalanyl, and leucyl residues; synthesized in the pancreas as chymotrypsinogen, and subsequently converted to π-, δ-, and finally α-chymotrypsin by successive trypsin-dependent cleavages; proposed for use in the treatment of inflammation and edema associated with trauma and to facilitate intracapsular cataract extraction; chymotrypsin A has the specificity described above, chymotrypsin B is homologous to chymotrypsin A, and chymotrypsin C has a broader specificity (for example, it acts additionally on carboxyl links of methionyl, glutaminyl, and asparaginyl residues).
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.
A pancreatic digestive enzyme that catalyzes the hydrolysis of certain proteins in the small intestine into polypeptides and amino acids.
chy′mo·tryp′tic (-tĭk) adj.
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.
chymotrypsinPhysiology A GI tract serine protease synthesized in the pancreas as a prohormone, which cleaves proteins at hydrophobic amino acids–leucine, phenylalanine, tryptophan, tyrosine
A serine proteinase of the gastrointestinal tract, synthesized in the pancreas as chymotrypsinogen; used in the treatment of inflammation and edema associated with trauma and to facilitate intracapsular cataract extraction.
chymotrypsinAn ENZYME that breaks down (digests) protein to amino acids and simpler substances. It is secreted by the pancreas and released into the DUODENUM. The enzyme is also used to clean wounds and in an earlier form of cataract surgery to cut the suspensory ligament (zonules) of the cataractous lens.
chymotrypsinan enzyme found in the pancreatic juice of mammals that functions as an endopeptidase, catalysing the hydrolysis of PEPTIDE BONDS. It attacks the carboxyl groups of specific amino acids (phenylalanine, tyrosine, leucine, tryptophan, and methionine) and so produces large peptides. The enzyme works in the alkaline medium of the small intestine and is secreted by the pancreas in an inactive form.
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.
a test of pancreatic exocrine efficiency depending on the presence of chymotrypsin to split a peptide-para-aminobenzoic acid compound.