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  2. Enteropeptidase - Wikipedia

    en.wikipedia.org/wiki/Enteropeptidase

    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 .

  3. Trypsin inhibitor - Wikipedia

    en.wikipedia.org/wiki/Trypsin_inhibitor

    It is formed in the pancreas and activated to trypsin with enteropeptidase [6] Chymotrypsinogen is the inactive form of chymotrypsin and has similar functions as trypsin. The presence of trypsin inhibitor has been found to result in delayed growth as well as metabolic and digestive diseases. [ 7 ]

  4. Enterocyte - Wikipedia

    en.wikipedia.org/wiki/Enterocyte

    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 ...

  5. Cancer immunotherapy - Wikipedia

    en.wikipedia.org/wiki/Cancer_immunotherapy

    Cancer immunotherapy (immuno-oncotherapy) is the stimulation of the immune system to treat cancer, improving the immune system's natural ability to fight the disease. [1] It is an application of the fundamental research of cancer immunology (immuno-oncology) and a growing subspecialty of oncology.

  6. This blood test screens for 50 different types of cancer. Is ...

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    Having a super-sensitive multi-cancer screening tool that could actually save lives is the “holy grail” for cancer researchers and physicians. The aptly named health care company Grail claims ...

  7. Trypsinogen - Wikipedia

    en.wikipedia.org/wiki/Trypsinogen

    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.

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