Question

Trypsin inhibitor is a pancreatic polypeptide that binds trypsin with very high affinity. Trypsin inhibitor deficiency can cause pancreatitis (inflammation of the pancreas). In normal digestion, trypsin activates several zymogens or proenzymes in which organ?

O mouth
O stomach
O small intestine
O pancreas

Answer 1

Trypsin activates several zymogens or proenzymes in the small intestine, which is essential for protein digestion. The function of trypsin inhibitors is to prevent autodigestion of the pancreas by hindering premature enzyme activation. The answer is option C.

Step-by-step explanation:

Trypsin is a pancreatic protease that plays a crucial role in protein digestion by activating other zymogens or proenzymes. The normal function of trypsin inhibitors is to prevent the premature activation of these enzymes within the pancreas, thereby protecting this organ from autodigestion. When trypsinogen is released into the small intestine, it is converted into active trypsin by the intestinal brush border enzyme enteropeptidase.

Once activated, trypsin can further activate other proteolytic enzymes such as chymotrypsinogen and procarboxypeptidase, resulting in their respective active forms, chymotrypsin, and carboxypeptidase. This process ensures the efficient breakdown of proteins into smaller peptides and amino acids, which can then be absorbed through the small intestinal wall and utilized by the body.