trypsin

A proteolytic enzyme formed in the small intestine from trypsinogen by the action of enteropeptidase; a serine proteinase that hydrolyzes peptides, amides, esters, etc., at bonds of the carboxyl groups of l-arginyl or l-lysyl residues; it also produces the meromyosins.

- crystallized t. a purified preparation of the pancreatic enzyme; used as an adjunct to surgery for débridement of necrotic wounds and ulcers.

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tryp·sin 'trip-sən n

1) a crystallizable proteolytic enzyme that differs from pepsin in several ways (as in being most active in a slightly alkaline medium and in hydrolyzing esters as well as amides) and that is produced and secreted in the pancreatic juice in the form of inactive trypsinogen and activated in the intestine compare CHYMOTRYPSIN

2) a preparation from the pancreatic juice differing from pancreatin in containing principally proteolytic enzymes and used chiefly as a digestive and lytic agent

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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.

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tryp·sin (tripґsin) [EC 3.4.21.4] a serine endopeptidase that catalyzes cleavage of peptide bonds on the carboxyl side of either arginine or lysine. It is secreted by the pancreas as the proenzyme trypsinogen and converted to the active form in the small intestine by enteropeptidase; the active enzyme catalyzes the cleavage and activation of additional trypsinogen and other pancreatic proenzymes important to protein digestion.