A-CHYMOTRYPSIN TYPE VII TLCK TREATED

Description_x000D_ Application_x000D_ α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme._x000D_ Packaging_x000D_ 10, 25, 100 mg in glass bottle_x000D_ Biochem/physiol Actions_x000D_ 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. Its 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, α2-macroglobulin, 10 mM Cu2+ and Hg2+._x000D_ A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond._x000D_ Unit Definition_x000D_ One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C._x000D_ Preparation Note_x000D_ TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity._x000D_ Analysis Note_x000D_ Protein determined by A1%/280_x000D_ Other Notes_x000D_ View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer