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Proteolytic Activation of Digestive Enzymes
Chymotrypsinogen is the zymogen form of chymotrypsin. Chymotrypsinogen is synthesized in exocrine cells of the pancreas known as acinar cells. These acinar cells synthesize chymotrypsinogen and other digestive zymogens, store them in membrane-bound granules and release them from the apex portion of the cell during hormonal stimulation or when stimulated by an action potential. These zymogens then travel into the ducts, which eventually connect with the pancreatic duct that empties out into the duodenum of the small intestine. Once inside the duodenum, the digestive enzymes are activated and begin to elicit their response on protein and lipid macromolecules. In order to activate chymotrypsinogen, trypsin cleaves it at a single site (between arginine-15 and isoleucine-16). This produces activate pi-chymotrypsin, which then goes on to other pi-chymotrypsin molecules and removes two dipeptides to form the fully active alpha-chymotrypsin. Therefore active chymotrypsin consists of three separate chains that are connected by disulfide bridges. Trypsin is actually the master activator because it activates not only chymotrypsinogen but also other zymogens such as proelastase, procarboxypeptidase, prolipase and protrypsin. Trypsin is initially activated by an enzyme called enteropeptidase, which is produced by the cells of the small intestine.
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