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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).
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.
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.