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Chymotrypsin |
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Chymotrypsin is a pancreatic digestive enzyme that catalyzes the hydrolysis of certain proteins in the small intestine into polypeptides and amino acids. Chymotrypsin hydrolyzes the peptide bond of amino acids with large hydrophobic side chains, such as phenylalanine, tryptophan, and tyrosine. Along with other digestive enzymes of the pancreas, chymotrypsinogen is carried in the pancreatic juice through the pancreatic duct into the duodenum. There chymotrypsinogen is activated by another enzyme, trypsin, and by molecules of active chymotrypsin. It is selective for peptide bonds with aromatic or large hydrophobic side chains on the carboxyl side of this bond. Chymotrypsin also catalyzes the hydrolysis of ester bonds. Chymotrypsin is secreted by the pancreas as proenzyme chymotrypsinogen. Chymotrypsin is produced in the pancreas as the inactive, or zymogen, form chymotrypsinogen. Chymotrypsin, along with the other pancreatic enzymes, is most often used in the treatment of pancreatic insufficiency. Chymotrypsin is also used in the debridement and treatment of abscesses and ulcerations, in the liquefaction of mucous secretions, in ophthalmic cataract surgeries and therapy of eyeball hematomas and ophthalmorrhagias. |
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