MICROANATOMY

Detailed explanation-1: -Trypsin and chymotrypsin are proteolytic endopeptidases. They are secreted in inactive forms of trypsinogen and chymotrypsinogen. The enterokinase secreted by intestine converts inactive trypsinogen to trypsin.

Detailed explanation-2: -Abstract. Enteropeptidase converts trypsinogen into active trypsin, which not only hydrolyses some peptide bonds of food proteins but also activates a number of pancreatic zymogens.

Detailed explanation-3: -Once trypsinogen is released into the lumen of the small intestine, enterokinase produced by the duodenal mucosa converts trypsinogen into an active form, trypsin.

Detailed explanation-4: -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.