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Trypsin Function

In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into abate peptides. The peptide articles are again added anatomize into amino acids via added proteases, apprehension them accessible for assimilation into the claret stream. Tryptic assimilation is a all-important footfall in protein assimilation as proteins are about too ample to be captivated through the lining of the baby intestine.

Trypsin is produced as the abeyant zymogen trypsinogen in the pancreas. When the pancreas is angry by cholecystokinin, it is again buried into the aboriginal allotment of the baby civil (the duodenum) via the pancreatic duct. Once in the baby intestine, the agitator enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage. Auto catalysis can appear with trypsin application trypsinogen as the substrate. This activation apparatus is accepted for a lot of serine proteases, and serves to anticipate autodegradation of the pancreas.

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