Anti-Chymotrypsin (Hu Pancreas) Antibody

Chymotrypsin is a serine endopeptidase that is synthesized in the pancreatic acinar cells as chymotrypsinogen that is cleaved by trypsin to generate active chymotrypsin. Activation of chymotrypsinogen involves proteolytic cleavage at two sites. The resultant three chains are held together by five disulfide bonds. Chymotrypsin is reported to preferentially cleave peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). The aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. Two predominant forms of chymotrypsin have been described and are designated as chymotrypsin A and B. They display high degree of homology but have significantly different proteolytic characteristics. The active site residues in chymotrypsin are far apart in the primary sequence but are brought together in a crevice formed between the two protein domains.