Description

• General description: Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges.[1] It has an isoelectric pH of 8.97.
• Application: α-Chymotrypsinogen A from bovine pancreas has been used as model protein crystallization reproducibility studies.[2] It has also been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies.[3]
• Biochem/physiol Actions: Chymotrypsinogen A requires limited proteolysis for its activation. Chymotrypsinogen A may be activated by trypsin and chymotrypsin (autolytic activation) to form m α, β, γ, δ and π chymotrypsin (depending upon the conditions of activation).[7] Chymotrypsin is a protease that will preferentially cleave peptides on the carboxyl side of aromatic amino acids including tryptophan, tyrosine, and phenylalanine. It will also hydrolyze peptides on the carboxyl side of leucine, methionine, and alanine.[8]
• Unit Definition: After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
• Other Notes: View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer