How is pepsinogen activated?a. It is activated by trypsin 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. Pepsinogen is activated by enteropeptidase through proteolytic cleavage. Enteropeptidase is an enzyme produced by the duodenal mucosa that activates trypsinogen to trypsin. Once activated, trypsin catalyzes the activation of pancreatic enzymes including chymotrypsinogen and procarboxypeptidase to chymotrypsin and carboxypeptidase, respectively. In addition, trypsin can also activate pepsinogen to pepsin, which is the active form of the enzyme that helps with the digestion of proteins in the stomach.
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