C. A or B; a serine proteinase of the gastrointestinal tract that preferentially cleaves carboxyl links of hydrophobic amino acid s, particularly at tyrosyl, tryptophanyl, phenylalanyl, and leucyl residues; synthesized in the pancreas as chymotrypsinogen, and subsequently converted to π-, δ-, and finally α-c. by successive trypsin-dependent cleavages; proposed for use in the treatment of inflammation and edema associated with trauma and to facilitate intracapsular cataract extraction; c. A has the specificity above, c. B is homologous to c. A, and c. C has a broader specificity ( e.g., additionally acting on carboxyl links of methionyl, glutaminyl, and asparaginyl residues).
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chy·mo·tryp·sin .kī-mō-'trip-sən n a protease that hydrolyzes peptide bonds and is formed in the intestine from chymotrypsinogen compare TRYPSIN
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n.
a protein-digesting enzyme (see peptidase). It is secreted by the pancreas in an inactive form, chymotrypsinogen, that is converted into chymotrypsin in the duodenum by the action of trypsin.
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chy·mo·tryp·sin (ki″mo-tripґsin) 1. [EC 3.4.21.1] a serine endopeptidase that preferentially cleaves peptide bonds on the carboxyl side of amino acids with bulky hydrophobic residues, particularly tyrosine, tryptophan, phenylalanine, and leucine. It is secreted by the pancreas as the inactive proenzyme chymotrypsinogen. 2. [USP] a proteolytic enzyme preparation crystallized from an extract of ox pancreas, used for enzymatic zonulolysis in intracapsular lens extraction. It has also been used to debride necrotic lesions and to reduce inflammation and edema; administered orally, buccally, or intramuscularly.Medical dictionary. 2011.