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trypsin
Trypsin () is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins.〔The German physiologist Wilhelm Kühne (1837-1900) discovered trypsin in 1876. See: W. Kühne (1877) "(Über das Trypsin (Enzym des Pankreas) )", ''Verhandlungen des naturhistorisch-medicinischen Vereins zu Heidelberg'', new series, vol. 1, no. 3, pages 194-198.〕 Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.
== Function ==
In the duodenum, trypsin catalyzes the hydrolysis of peptide bonds, breaking down proteins into smaller peptides. The peptide products are then further hydrolyzed into amino acids via other proteases, rendering them available for absorption into the blood stream. Tryptic digestion is a necessary step in protein absorption as proteins are generally too large to be absorbed through the lining of the small intestine.
Trypsin is produced as the inactive zymogen trypsinogen in the pancreas. When the pancreas is stimulated by cholecystokinin, it is then secreted into the first part of the small intestine (the duodenum) via the pancreatic duct. Once in the small intestine, the enzyme enteropeptidase activates trypsinogen into trypsin by proteolytic cleavage. Auto catalysis can happen with trypsin using trypsinogen as the substrate. This activation mechanism is common for most serine proteases, and serves to prevent autodegradation of the pancreas.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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