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+.
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.
Unit Definition
One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
CHM.NJE0002 - α-Chymotrypsin from bovine pancreas - CAS: 9004-07-3
Synonyms(s): α-Chymotrypsin (bovine); Chymotrypsin (bovine); TLCK-Chymotrypsin
CAS number: 9004-07-3Level: USP level
Molecular weight: 25KDa
Specific Activity: ≥1500USP units/mg
Definition of activity: 25℃, PH7.0, reduce the optical density value at 237nm per minute by 0.001, and the amount of enzyme is 1ATEE unit (u)
Loss on dry weight: ≤5.0%Burning residue: ≤2.5%
Shape: white or nearly white crystalline or amorphous powder. No smell. Soluble in water and dilute buffer solution. The optimum pH is 7.5 to 8.5. Isoelectric point (PI) 8.3. Half lethal dose (rat, vein) 84mg/kg. It is a proteolytic enzyme that can preferentially hydrolyze the peptide bonds formed by the carboxyl groups of L-tyrosine and L-phenylalanine. The activity of chymin is inhibited to varying degrees by heavy metals and natural trypsin inhibitors.
Use: biochemical research. Decomposition and digestion of protein. Proteolytic enzyme is used for protein hydrolysis without the presence of exogenous trypsin activity. It has the effect of breaking down peptide bonds, and the carboxyl end of the hydrolyzed peptide bond has a peptide bond of aromatic or long hydrophobic chain (Tyr, Trp, Phe, Met).
Store at: -20℃
