SERPINA3-1 antikoerper, Pi2 antikoerper, AACT antikoerper, ACT antikoerper, GIG25 antikoerper, A1AT antikoerper, PI antikoerper, alpha-1-PI antikoerper, AAT antikoerper, Pi antikoerper, Spi1 antikoerper, SERPINA3-5 antikoerper, serpina3 antikoerper, serpin A3-5 antikoerper, serpin family A member 3 antikoerper, alpha-1-antiproteinase F precursor antikoerper, serpin family A member 1 antikoerper, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5 antikoerper, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 antikoerper, serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 L homeolog antikoerper, LOC396684 antikoerper, SERPINA3 antikoerper, LOC100008973 antikoerper, SERPINA1 antikoerper, Serpina1 antikoerper, SPIA5 antikoerper, serpina3.L antikoerper
Hintergrund
Chymotrypsins, such as Chymotrypsin C (also known as pancreatic Chymotrypsin or Chymotrypsin), are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the un-reactive carbonyl group with a powerful nucleophile, the Serine 195 residue located in the active site of the enzyme, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin C is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive, but becomes active as a three polypeptide molecule that is interconnected by disulfide bonds.Synonyms: AACT, Cell growth-inhibiting gene 24/25 protein, GIG24, GIG25, SERPINA3