Pepsin, 1:10,000
Product Name | Pepsin, 1:10,000 powder |
Source | Porcine Gastric Mucosa |
Catalogue Number | 441-10 |
Purity | Partially Purified |
Form | Powder |
Activity | >10,000 U/mg |
Aerobic Plate Count | < 10,000 CFU/g |
Loss on Drying | < 4% |
pH | 3.0 - 4.5 (2% solution) |
Salmonella sp. | Negative |
E. coli | Negative |
Appearance | Off-white to tan powder |
Related Products | 440-50 - Pepsinogen I from human gastric mucosa 440-52 - Pepsinogen II from human gastric mucosa 435-10 - Mucin from porcine gastric mucosa |
Storage | 2-8°C |
Recertification | 3 years |
CAS Number | 9001-75-6 |
E.C. Number | 3.4.23.1 |
Country of Origin | United States of America |
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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 the first enzyme to be discovered, and, in 1929, 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.
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.