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Pepsin
Pepsin is an enzyme whose zymogen (pepsinogen) is released by the chief cells in the stomach and that degrades food proteins into peptides. It was discovered in 1836 by Theodor Schwann who also coined its name from the Greek word ''pepsis'', meaning "digestion" (from ''peptein'' "to digest").〔, .〕 It was one of the first enzymes to be discovered, and, in 1928, it became one of the first enzymes to be crystallized, by John H. Northrop. Pepsin is a digestive protease, a member of the aspartate protease family.〔(【引用サイトリンク】 url=http://www.expasy.org/cgi-bin/nicezyme.pl?3.4.23.1 )〕
Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system, the other two being chymotrypsin and trypsin. The three enzymes were among the first to be isolated in crystalline form. During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the intestinal lining. Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.
== History ==
The term "pepsin" was first coined by Theodor Schwann in the early 19th century. Scientists around this time began discovering many biochemical compounds that play a significant role in biological processes and pepsin was one of them. This acidic substance that was able to convert nitrogen based foods into water-soluble material was determined to be pepsin.
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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