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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.
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.
This produces a bolus which is swallowed down the esophagus to enter the stomach. The second stage, the gastric phase, happens in the stomach. Here, the food is further broken down by mixing with gastric acid until it passes into the duodenum, the first part of the small intestine. The third stage, the intestinal phase, begins in the duodenum.
Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases.. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney.
The cud is then regurgitated, chewed slowly to completely mix it with saliva and to break down the particle size. Fibre, especially cellulose and hemi-cellulose, is primarily broken down into the volatile fatty acids, acetic acid, propionic acid and butyric acid in these chambers (the reticulo-rumen) by microbes: (bacteria, protozoa, and fungi ...
The arrangement of these proteins on the apical and basolateral sides of the epithelium determines the net movement of ions and water in the tract. H + and Cl − are secreted by the parietal cells into the lumen of the stomach creating acidic conditions with a low pH of 1. H + is pumped into the stomach by exchanging it with K +.
The proenzyme Pepsinogen, with the exposure to hydrochloric acid gets converted into the active enzyme pepsin, the proteolytic enzyme of the stomach. Hydrochloric acid (HCl) provides the acidic pH (pH 1.8) optimal for pepsins. Rennin is a proteolytic enzyme found in gastric juice of infants which helps in the digestion of milk proteins.
Secretin is used in diagnostic tests for pancreatic function; secretin is injected and the pancreatic output can then be imaged with magnetic resonance imaging, a noninvasive procedure, or secretions generated as a result can gathered either through an endoscope or through tubes inserted through the mouth, down into the duodenum. [36] [37] [38]