HUMAN PHYSIOLOGY
DIGESTION AND ABSORPTION
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Question
[CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
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Trypsin is secreted by pancreas as zymogen
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Large peptides and few amino acids are products of protein hydrolysis
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Pepsinogen are activated by autocatalysis
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Most of the digested protein are absorbed in intestine as polypeptides
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Enterokinase activate pancreatic zymogens
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Detailed explanation-1: -Enterokinase is a protease of the intestinal brush border that specifically cleaves the acidic propeptide from trypsinogen to yield active trypsin. This cleavage initiates a cascade of proteolytic reactions leading to the activation of many pancreatic zymogens.
Detailed explanation-2: -In the small intestine, pancreatic zymogen activation begins with the conversion of trypsinogen to trypsin by the intestinal brush-border protease enterokinase.
Detailed explanation-3: -Small Intestine Pancreatic trypsinogen is secreted in the intestine by the pancreas in an inactive form but becomes activated by the enzyme enterokinase, a brush border enzyme in the duodenum to an activated form of trypsin. Trypsin then activates the other pancreatic proteolytic enzyme precursors.
Detailed explanation-4: -Luminal digestion of dietary proteins begins in the stomach and is initiated by pepsin that is secreted by chief cells, deep in the mucosal crypts. Pepsin is released into the lumen in the form of inactive precursor (zymogen) known as pepsinogen.
Detailed explanation-5: -Enteropeptidase (enterokinase) is an enzyme secreted from intestinal glands (the crypts of Lieberkuhn) following the entry of ingested food passing from the stomach. It converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.