1. 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-, ΄-, 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 (it acts additionally on carboxyl links of methionyl, glutaminyl, and asparaginyl residues).
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