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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]
An antibody digested by pepsin yields two fragments: a F(ab') 2 fragment and a pFc' fragment The variable regions of the heavy and light chains can be fused together to form a single-chain variable fragment (scFv), which is only half the size of the Fab fragment, yet retains the original specificity of the parent immunoglobulin.
The human stomach has receptors responsive to sodium glutamate [40] and this information is passed to the lateral hypothalamus and limbic system in the brain as a palatability signal through the vagus nerve. [41] The stomach can also sense, independently of tongue and oral taste receptors, glucose, [42] carbohydrates, [43] proteins, [43] and ...
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 ...
Secretin and its receptor are found in discrete nuclei of the hypothalamus, including the paraventricular nucleus and the arcuate nucleus, which are the primary brain sites for regulating body energy homeostasis. It was found that both central and peripheral injection of Sct reduce food intake in mouse, indicating an anorectic role of the peptide.
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 damage the stomach wall, mucus is secreted by innumerable gastric glands in the stomach, to provide a slimy protective layer against the damaging effects ...
This led to the conclusion that papain cleaves on the amino-terminal side of the disulfide bond, and pepsin cleaves on the carboxyl-terminal side. Nisonoff's work also contributed to the identification of the F(ab’)2 fragment of the antibody molecule, which is the single bivalent fragment that is produced after pepsin cleavage.
Some antacids also inhibit pepsin, an enzyme that can damage the esophagus in acid reflux. [2] [13] Antacids do not directly inhibit acid secretion, and thus are distinct from acid-reducing drugs like H 2-receptor antagonists or proton pump inhibitors. [4] Antacids do not kill the bacteria Helicobacter pylori, which causes most ulcers. [4]