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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. Trypsin 1 - Wikipedia

    en.wikipedia.org/wiki/Trypsin_1

    Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2 (anionic trypsinogen), and trypsin-3 (meso-trypsinogen).

  4. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    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]

  5. Trypsin inhibitor - Wikipedia

    en.wikipedia.org/wiki/Trypsin_inhibitor

    A trypsin inhibitor (TI) is a protein and a type of serine protease inhibitor that reduces the biological activity of trypsin by controlling the activation and catalytic reactions of proteins. [1] Trypsin is an enzyme involved in the breakdown of many different proteins , primarily as part of digestion in humans and other animals such as ...

  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. Trypsinogen - Wikipedia

    en.wikipedia.org/wiki/Trypsinogen

    Trypsin is produced, stored and released as the inactive trypsinogen to ensure that the protein is only activated in the appropriate location. Premature trypsin activation can be destructive and may trigger a series of events that lead to pancreatic self-digestion.

  8. Enteropeptidase - Wikipedia

    en.wikipedia.org/wiki/Enteropeptidase

    Enteropeptidase exhibits trypsin-like activity, cleaving proteins following a lysine at a specific cleavage site (Asp-Asp-Asp-Asp-Lys). [19] This cleavage results in trypsindependent activation of other pancreatic zymogens, such as chymotrypsinogen, proelastase, procarboxypeptidase and prolipase in the lumen of the gut. [20]

  9. Alpha-1 antitrypsin - Wikipedia

    en.wikipedia.org/wiki/Alpha-1_antitrypsin

    Alpha-1 antitrypsin or α 1-antitrypsin (A1AT, α 1 AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded in humans by the SERPINA1 gene.A protease inhibitor, it is also known as alpha 1 –proteinase inhibitor (A1PI) or alpha 1-antiproteinase (A1AP) because it inhibits various proteases (not just trypsin). [5]

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