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Pepsin / ˈ p ɛ p s ɪ n / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. [2]
Pepsin is the main gastric enzyme. It is produced in the stomach by gastric chief cells in its inactive form pepsinogen, which is a zymogen. Pepsinogen is then activated by the stomach acid into its active form, pepsin. Pepsin breaks down the protein in the food into smaller particles, such as peptide fragments and amino acids.
A prime example of this is pepsin, which is secreted in the stomach by chief cells. Pepsin in its secreted form is inactive . However, once it reaches the gastric lumen it becomes activated into pepsin by the high H+ concentration, becoming an enzyme vital to digestion. The release of the enzymes is regulated by neural, hormonal, or paracrine ...
The gastric mucosa is covered in surface mucous cells that produce the mucus necessary to protect the stomach's epithelial lining from gastric acid secreted by parietal cells in the glands, and from pepsin, a secreted digestive enzyme. Surface mucous cells follow the indentations and partly line the gastric pits.
The gastric chief cell (also known as a zymogenic cell or peptic cell) is a cell in the stomach that releases pepsinogen [1] and chymosin.Pepsinogen is activated into the digestive enzyme pepsin when it comes in contact with hydrochloric acid produced by gastric parietal cells. [2]
A peptide hormone, gastrin, produced by G cells in the gastric glands, stimulates the production of gastric juice which activates the digestive enzymes. Pepsinogen is a precursor enzyme produced by the gastric chief cells, and gastric acid activates this to the enzyme pepsin which begins the digestion of proteins. As these two chemicals would ...
This gene encodes a protein precursor of the digestive enzyme pepsin, a member of the peptidase A1 family of endopeptidases. The encoded precursor is secreted by gastric chief cells and undergoes autocatalytic cleavage in acidic conditions to form the active enzyme, which functions in the digestion of dietary proteins.
Discovered in 1836, pepsin was one of the first enzymes to be classified as an exoenzyme. [8] The enzyme is first made in the inactive form, pepsinogen by chief cells in the lining of the stomach. [24] With an impulse from the vagus nerve, pepsinogen is secreted into the stomach, where it mixes with hydrochloric acid to form pepsin. [25]