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  2. Carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase

    Some, but not all, carboxypeptidases are initially produced in an inactive form; this precursor form is referred to as a procarboxypeptidase. In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin. This mechanism ensures that ...

  3. Carboxypeptidase A2 - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_A2

    Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene. [5] [6] [7]Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties.

  4. Carboxypeptidase A - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_A

    Carboxypeptidase A is produced in the pancreas and is crucial to many processes in the human body to include digestion, post-translational modification of proteins, blood clotting, and reproduction. Applications

  5. Pancreatic juice - Wikipedia

    en.wikipedia.org/wiki/Pancreatic_juice

    Pancreatic juice secretion is principally regulated by the hormones secretin and cholecystokinin, which are produced by the walls of the duodenum, and by the action of autonomic innervation. The release of these hormones into the blood is stimulated by the entry of the acidic chyme into the duodenum. Their coordinated action results in the ...

  6. CPA3 - Wikipedia

    en.wikipedia.org/wiki/CPA3

    CPA3 has a pH optimum in the neutral to basic range. CPA3 functions together with endopeptidases secreted from mast cells such as chymases and tryptases to degrade proteins and peptides, including the apolipoprotein B component of LDL particles and angiotensin I. [9] [10] Upon mast cell activation and degranulation, CPA3, the chymases, and tryptases are released in complexes with heparin ...

  7. Protease - Wikipedia

    en.wikipedia.org/wiki/Protease

    Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]

  8. Zymogen - Wikipedia

    en.wikipedia.org/wiki/Zymogen

    In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.

  9. 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.