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Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes.
Gastrointestinal physiology is the branch of human physiology that addresses the physical function of the gastrointestinal (GI) tract.The function of the GI tract is to process ingested food by mechanical and chemical means, extract nutrients and excrete waste products.
The gastrointestinal tract (GI tract, digestive tract, alimentary canal) is the tract or passageway of the digestive system that leads from the mouth to the anus.The GI tract contains all the major organs of the digestive system, in humans and other animals, including the esophagus, stomach, and intestines.
The human digestive system consists of the gastrointestinal tract plus the accessory organs of digestion (the tongue, salivary glands, pancreas, liver, and gallbladder). Digestion involves the breakdown of food into smaller and smaller components, until they can be absorbed and assimilated into the body.
Pepsin breaks down the protein in the food into smaller particles, such as peptide fragments and amino acids. Protein digestion, therefore, primarily starts in the stomach, unlike carbohydrate and lipids, which start their digestion in the mouth (however, trace amounts of the enzyme kallikrein , which catabolises certain protein, is found in ...
In the human digestive system, a bolus (a small rounded mass of chewed up food) enters the stomach through the esophagus via the lower esophageal sphincter. The stomach releases proteases (protein-digesting enzymes such as pepsin), and hydrochloric acid, which kills or inhibits bacteria and provides the acidic pH of 2 for the proteases to work.
Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.
Proteolysis of the zymogen yields an active protein; for example, when trypsinogen is cleaved to form trypsin, a slight rearrangement of the protein structure that completes the active site of the protease occurs, thereby activating the protein.