Trypsin, human

Trypsin, an enzyme that degrades proteins, 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)brings out its maximum 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 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, and 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 sequences of various proteins; trypsin is widely employed as a reagent for the orderly and unambiguous cleavage of such molecules.