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Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the ...
Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. When the pancreas is stimulated by cholecystokinin , it is then secreted into the first part of the small intestine (the duodenum ) via the pancreatic duct .
The pancreas also receives autonomic innervation. The blood flow into pancreas is regulated by sympathetic nerve fibers, while parasympathetic neurons stimulate the activity of acinar and centroacinar cells. Pancreatic secretion is an aqueous solution of bicarbonate originating from the duct cells and enzymes originating from the acinar cells.
Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin.
Secretin, a hormone produced by the duodenal "S cells" in response to the stomach chyme containing high hydrogen atom concentration (high acidity), is released into the blood stream; upon return to the digestive tract, secretion decreases gastric emptying, increases secretion of the pancreatic ductal cells, as well as stimulating pancreatic ...
1. Chocolate Fondue. Think of that fondue fountain at the buffet as Willy Wonka's sacred chocolate waterfall and river. The chocolate must go untouched by human hands, or it will be ruined.
This prevents damage to the pancreas or any other organs. It is activated into its active form by another enzyme called trypsin. This active form is called π-chymotrypsin and is used to create α-chymotrypsin. Trypsin cleaves the peptide bond in chymotrypsinogen between arginine-15 and isoleucine-16. This creates two peptides within the π ...