How is trypsinogen activated?a. It is activated by pepsin through proteolytic cleavage.b. It is activated by enteropeptidase through proteolytic cleavage.c. It is activated by low pH which causes auto-proteolytic cleavage.d. It is activated by high pH which causes auto-proteolytic cleavage.
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The correct answer is b. Trypsinogen is an inactive precursor of trypsin, which is a proteolytic enzyme involved in protein digestion. Trypsinogen is activated by a specific protease called enteropeptidase, which is located on the brush border of the small intestine.
When chyme (partially digested food) enters the duodenum (first part of the small intestine), it stimulates the release of enteropeptidase from the duodenal cells. Enteropeptidase then cleaves the N-terminal peptide of trypsinogen, converting it to active trypsin. Once active, trypsin can then activate other pancreatic enzymes and continue the digestive process.
Pepsin, which is also a protease, is not involved in the activation of trypsinogen. Low pH and high pH do not activate trypsinogen through auto-proteolytic cleavage.
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