Description_x000D_ General description_x000D_ Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges. It has an isoelectric pH of 8.97._x000D_ Application_x000D_ The enzyme from Sigma has been used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy. It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. The enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. In this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution._x000D_ α-Chymotrypsinogen A from bovine pancreas has been used as model protein crystallization reproducibility studies. It has also been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies._x000D_ Packaging_x000D_ 1, 5 g in poly bottle_x000D_ 100, 250 mg in poly bottle_x000D_ Biochem/physiol Actions_x000D_ 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). 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._x000D_ A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond._x000D_ Unit Definition_x000D_ After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C._x000D_ Other Notes_x000D_ View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer