An enzyme of pancreatic juice that hydrolyzes proteins into smaller polypeptide units.
A serine endopeptidase that is formed from trypsinogen in the pancreas. It is converted into its active form by enteropeptidase in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine.
A proteolytic enzyme of the pancreatic juice, an endopeptidase.
An enzyme from the pancreas used to tenderize meats.
A proteolytic (protein chain-cutting) enzyme that is produced by the pancreas. Trypsin cleaves polypeptide (protein) molecular chains on the carboxyl (group) side of arginine and lysine units (residues).
An enzyme converted from trypsinogen by the duodenum and secreted into the digestive system where it absorbs protein.
A proteolytic enzyme that attacks peptide bonds adjacent to arginine or lysine.
Enzyme involved in the digestion of proteins. The inactive form, trypsinogen, is secreted by the pancreas and converted to active trypsin in the duodenum.
An enzyme that continues the digestion of proteins by breaking down peptones into smaller peptide chains. 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.
The chief protein enzyme of the pancreatic secretion. Secreted by the pancreas as trypsinogen (an inactive form), it is converted in the duodenum by another enzyme, enteropeptidase. It changes proteins into peptones and forms the main constituent of pancreatic extracts used for digestion of food.
A proteolytic enzyme formed in the intestine from trypsinogen. It catalyzes the hydrolysis of peptide bonds in partly digested proteins and some native proteins, the final products being amino acids and various polypeptides.
This is a specific kind of enzyme released by the pancreas, crucial for digestion as it helps in breaking down proteins.
An enzyme secreted by the pancreas that transforms proteins into peptones and polypeptides; it plays a role in the digestion of proteins.