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  2. Trypsin - Wikipedia

    en.wikipedia.org/wiki/Trypsin

    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.

  3. Endopeptidase - Wikipedia

    en.wikipedia.org/wiki/Endopeptidase

    Trypsin - cuts after Arg or Lys, unless followed by Pro. Very strict. Works best at pH 8. Chymotrypsin - cuts after Phe, Trp, or Tyr, unless followed by Pro. Cuts more slowly after His, Met or Leu. Works best at pH 8. Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro.

  4. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    As a result, the zymogen trypsinogen breaks down into trypsin. Recall that trypsin is also responsible for cleaving lysine peptide bonds, and thus, once a small amount of trypsin is generated, it participates in cleavage of its own zymogen, generating even more trypsin. The process of trypsin activation can thus be called autocatalytic.

  5. Trypsinogen - Wikipedia

    en.wikipedia.org/wiki/Trypsinogen

    Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme.It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.

  6. Trypsinization - Wikipedia

    en.wikipedia.org/wiki/Trypsinization

    Trypsinization is the process of cell dissociation using trypsin, a proteolytic enzyme which breaks down proteins, to dissociate adherent cells from the vessel in which they are being cultured. When added to cell culture, trypsin breaks down the proteins that enable the cells to adhere to the vessel.

  7. Tosyl phenylalanyl chloromethyl ketone - Wikipedia

    en.wikipedia.org/wiki/Tosyl_phenylalanyl_chloro...

    TPCK-treated trypsin is used to improve infection yield in laboratory tissue culture of some wild virus isolates that are not well-adapted to growth in vitro, such as some low-pathogenic avian influenza strains or fresh clinical isolates of SARS-CoV-2. The trypsin performs the maturation cleavage of the viral envelope proteins efficiently.

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  9. 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.

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