APPLIED RADIOLOGICAL ANATOMY

Detailed explanation-1: -Trypsinogen is activated by enterokinase, which cleaves an amino-terminal activation peptide (TAP). Active trypsin then cleaves and activates all of the other pancreatic proteases, a phospholipase, and colipase, which is necessary for the physiological action of pancreatic triglyceride lipase.

Detailed explanation-2: -In healthy subjects, the 3 known pancreatic trypsinogens, which are endopeptidases belonging to the chymotrypsin superfamily, are activated by enterokinase and partial autoactivation in the duodenum.

Detailed explanation-3: -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-4: -Mild protein digestion by hydrochloric acid and proteolytic enzymes begins in the stomach. Enterokinase is produced by the duodenal mucosa. It activates trypsin, a pancreatic proteolytic enzyme, which in turn activates the remainder of the enzymes facilitating protein digestion.

Detailed explanation-5: -Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes.