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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 .
Enteropeptidase (also known as enterokinase) is responsible for activating pancreatic trypsinogen into trypsin, which activates other pancreatic zymogens. They are involved in the Krebs and the Cori Cycles and can be synthesized with lipase. Lipid uptake. Lipids are broken down by pancreatic lipase aided by bile, and then diffuse into the ...
If a true outbreak is discovered, infection control practitioners try to determine what permitted the outbreak to occur, and to rearrange the conditions to prevent ongoing propagation of the infection. Often, breaches in good practice are responsible, although sometimes other factors (such as construction) may be the source of the problem.
Of the study participants, women were at a higher risk of developing dementia than men, but they also had a better response to the vitamin D intervention—women who took it had a 49% lower risk ...
Post-exposure prophylaxis, also known as post-exposure prevention (PEP), is any preventive medical treatment started after exposure to a pathogen in order to prevent the infection from occurring. It should be contrasted with pre-exposure prophylaxis , which is used before the patient has been exposed to the infective agent.
Trypsinogen is activated by enteropeptidase (also known as enterokinase). Enteropeptidase is produced by the mucosa of duodenum and it cleaves the peptide bond of trypsinogen after residue 15, which is a lysine. The N-terminal peptide is discarded, and a slight rearrangement of the folded protein occurs.