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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 .
In women where the pregnancy is not the first, malaria infection is more often asymptomatic, even at high parasite loads, compared to women having their first pregnancy. [1] There is a decreasing susceptibility to malaria with increasing parity, probably due to immunity to pregnancy-specific antigens. [1] Young maternal age and increases the ...
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 ...
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.
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.
Immune tolerance in pregnancy or maternal immune tolerance is the immune tolerance shown towards the fetus and placenta during pregnancy. This tolerance counters the immune response that would normally result in the rejection of something foreign in the body, as can happen in cases of spontaneous abortion .
Hypercoagulability in pregnancy is the propensity of pregnant women to develop thrombosis (blood clots) such as a deep vein thrombosis with a potential subsequent pulmonary embolism. Pregnancy itself is a factor of hypercoagulability (pregnancy-induced hypercoaguability), as a physiologically adaptive mechanism to prevent post partum bleeding. [7]
Crystal structure of Trypsin, a typical serine protease.. Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. [1]