Tripsín

Tripsín is a digestive enzyme that plays a crucial role in the breakdown of proteins within the body. It is synthesized in the pancreas as an inactive precursor called tripsinogen. Upon reaching the small intestine, tripsinogen is converted into its active form, tripsin, by another enzyme called enterokinase.

Once activated, tripsin functions by cleaving peptide bonds in proteins, specifically targeting the peptide bonds that follow lysine or arginine amino acid residues. This enzymatic activity breaks down large protein molecules into smaller peptides and amino acids, which can then be absorbed by the intestinal lining and utilized by the body for various functions, including building and repairing tissues, producing enzymes, and synthesizing hormones.

Besides its digestive function, tripsin also plays a role in other physiological processes. It is involved in blood clotting, as it can activate other clotting factors. Furthermore, it has been studied for its potential therapeutic applications, such as in the treatment of certain inflammatory conditions or for breaking down scar tissue. The precise regulation of tripsin activity is essential to prevent the digestion of the pancreatic cells themselves, which is achieved through the production of inhibitory molecules.