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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

    The presence of trypsin inhibitor has been found to result in delayed growth as well as metabolic and digestive diseases. [7] Additionally, pancreatic hypertrophy is a common occurrence with trypsin inhibitor consumption [ 8 ] The presence of trypsin inhibitor in a product reduces the protein efficiency and therefore results in the consumers ...

  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. A key protein may help Ozempic users retain muscle mass ... - AOL

    www.aol.com/key-protein-may-help-ozempic...

    One big area of concern for users of GLP-1 medications such as Ozempic and Wegovy is preventing muscle loss during weight loss. Salk Institute researchers have identified that the protein BCL6 is ...

  6. Gastrointestinal hormone - Wikipedia

    en.wikipedia.org/wiki/Gastrointestinal_hormone

    Ghrelin agonistic treatments can be used to treat illnesses such as anorexia and loss of appetites in cancer patients. Ghrelin treatments for obesity are still under intense scrutiny and no conclusive evidence has been reached. This hormone stimulates growth hormone release. Amylin controls glucose homeostasis and gastric motility

  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.

  8. Protein (nutrient) - Wikipedia

    en.wikipedia.org/wiki/Protein_(nutrient)

    Protein is a nutrient needed by the human body for growth and maintenance. Aside from water, proteins are the most abundant kind of molecules in the body. Protein can be found in all cells of the body and is the major structural component of all cells in the body, especially muscle. This also includes body organs, hair and skin.

  9. D-peptide - Wikipedia

    en.wikipedia.org/wiki/D-peptide

    The D-enantiomer protein (D-protein) is chemically synthesized from the same sequence using D-amino acids. If the target L-protein does not require a chaperone or co-factor to fold, the D-protein will mirror the conformation and properties of the L-protein, but the L-peptide inhibitor will most likely have little binding affinity towards it.