α-Chymotrypsin−Agarose from bovine pancreas lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units) Sigma C9134
Analysis Note
Protein determined by A
Biochem/physiol Actions
Serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the bond.
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+.
Packaging
50, 100 units in poly bottle
Unit Definition
One unit will hydrolyze 1.0 μmole of N-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 8.0 at 30 °C.
Physical form
Stabilized with lactose
Application
α-Chymotrypsin agarose from bovine pancreas has been used to study the purification and characterization of glucoamylase. α-Chymotrypsin agarose from bovine pancreas has also been used in a study to investigate molecular modeling for the design of a biomimetic chimeric ligand.
Характеристики реактива | |
storage temp. | −20°C |