Description

• Application: The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE).[1]
• Biochem/physiol Actions: α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.
• Unit Definition: One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
• Preparation Note: Produced from 3× crystallized chymotrypsinogen
• Analysis Note: Protein determined by E1%/280
• Other Notes: View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer