trypsin An enzyme that digests proteins (see endopeptidase; protease). It is secreted in an inactive form (trypsinogen) by the pancreas into the duodenum. There, trypsinogen is acted on by an enzyme (enterokinase) produced in the brush border of the duodenum to yield trypsin. The active enzyme plays an important role in the digestion of proteins in the anterior portion of the small intestine. It also activates other proteases in the pancreatic juice (see carboxypeptidase; chymotrypsin).

trypsin Digestive enzyme secreted by the pancreas. It is secreted in an inactive form that is converted into active trypsin by an enzyme in the small intestine. It breaks down peptide bonds on the amino acids lysine and arginine. See also alimentary canal; digestion; digestive system

trypsin A proteinase (endopeptidase) enzyme that acts primarily on the interior bonds of proteins. It is produced in the pancreas as the inactive zymogen trypsinogen, which on secretion into the intestine is converted into the active form by the intestinal enzyme enterokinase.

trypsin A proteolytic enzyme of the pancreatic juice, an endopeptidase. Active at alkaline pH (8–11). Secreted as the inactive precursor, trypsinogen, which is activated by enteropeptidase.

trypsin chief digestive enzyme of the pancreatic juice. XIX. perh. for *tripsin, f. Gr. trîpsis rubbing, f. tríbein rub; so named because first obtained by rubbing down the pancreas with glycerin; see -IN.