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trypsin

The Columbia Encyclopedia, Sixth Edition | Date: 2008

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 p H 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.

Author not available, TRYPSIN., The Columbia Encyclopedia, Sixth Edition 2008



The Columbia Encyclopedia, Sixth Edition. Copyright 2008 Columbia University Press

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Related entries from encyclopedias, dictionaries, and thesauruses

trypsin inhibitors
A Dictionary of Food and Nutrition trypsin inhibitors Proteins in soya and other beans which inhibit trypsin ; they are denatured and hence inactivated by heating. Read more
trypsin
World Encyclopedia 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 Read more
trypsinogen
A Dictionary of Food and Nutrition trypsinogen The inactive precursor of trypsin , secreted in the pancreatic juice. Read more
ovomucoid
A Dictionary of Food and Nutrition ovomucoid A protein of egg-white, 12% of the total solids. It inhibits the digestive enzyme trypsin , but is inactivated by pepsin in the stomach. Read more
Control Mechanisms
Biology ... cleavage becomes the digestive enzyme trypsin. Trypsinogen is made in the pancreas and ... called enteropeptidase. The small amount of trypsin made by enteropeptidase then goes on to ... molecules of trypsinogen to make more trypsin as well as cleaving the other pancreatic ... Read more

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Trypsinisation of 3t3 cells, timelapse