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Encyclopedia > Pepsinogen

Pepsin is a protease, a digestive enzyme that degrades food proteins in the stomach; the other important digestive enzymes are trypsin and chymotrypsin. It was the first animal enzyme to be discovered, by Theodor Schwann in 1836.


Pepsin is expressed as a pro-form, pepsinogen with an additional 44 amino acids, which are cleaved off outside the secreting cell, to avoid digestion of cellular proteins.


Pepsin is most active at pH 2-4. It is permanently inactivated above pH 6.


The name Pepsi is derived from pepsin. Pepsin is also used in the preparation of cheese.


External links

  • Pepsin product information from China GreatVista Chemicals (http://www.greatvistachemicals.com/biochemicals/pepsin.html)

  Results from FactBites:
 
Stomach - Wikipedia, the free encyclopedia (918 words)
The cells at the base of these pits are chief cells, responsible for production of pepsinogen, an inactive precursor for pepsin, which degrades proteins.
Near the top of the pits, closest to the contents of the stomach, there are mucus producing cells called goblet cells that help protect the stomach from self-digestion.
The hormone gastrin causes an increase in the secretion of HCl, pepsinogen and intrinsic factor from parietal cells in the stomach.
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