trypsin,enzyme that acts to degrade protein; it is often referred to as a proteolytic enzyme, or proteinase. Trypsin is one of the three principal digestive proteinases, the other two being pepsin and chymotrypsin. In the digestive process, trypsin acts with the other proteinases to break down dietary protein molecules to their component peptides and amino acids. Trypsin continues the process of digestion (begun in the stomach) in the small intestine where a slightly alkaline environment (about pH 8) promotes its maximal enzymatic activity. Trypsin, produced in an inactive form by the pancreas, is remarkably similar in chemical composition and in structure to the other chief pancreatic proteinase, chymotrypsin. Both enzymes also appear to have similar mechanisms of action; residues of histidine and serine are found in the active sites of both. The chief difference between the two molecules seems to be in their specificity, that is, each is active only against the peptide bonds in protein molecules that have carboxyl groups donated by certain amino acids. For trypsin these amino acids are arginine and lysine, for chymotrypsin they are tyrosine, phenylalanine, tryptophan, methionine, and leucine. Trypsin is the most discriminating of all the proteolytic enzymes in terms of the restricted number of chemical bonds that it will attack. Good use of this fact has been made by chemists interested in the determination of the amino acid sequence of proteins; trypsin is widely employed as a reagent for the orderly and unambiguous cleavage of such molecules.
An enzyme that digests proteins (see endopeptidase
). 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
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
; digestive system
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.
enzyme of the pancreatic juice
, an endopeptidase
. Active at alkaline pH (8–11). Secreted as the inactive precursor, trypsinogen, which is activated by enteropeptidase.
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
trypsin (trip-sin) n.
an enzyme that continues the digestion of proteins by breaking down peptones into smaller peptide chains (see peptidase
). It is secreted by the pancreas in an inactive form, trypsinogen
, which is converted in the duodenum to trypsin by the action of the enzyme enteropeptidase.