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.
- Produced from 3x Crystallized chymotrypsinogen
- Used to treat pancreatic insufficiency
- Used in traumatology
Chymotrypsin preferentially catalyzes the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyzes at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.
Grade: 3X CRYSTALLIZED
Concentration: Protein: ≥80%
Specific Activity: ≥40 u/mg protein
Key Applications: Enzymes, Inhibitors, Substrates
Application Areas: Molecular Biology
Product Type: Proteins, Enzymes & Peptides
Gene Id: cow ... CTRB1(618826)
Extinction Coefficient (E1%): 20.4(Lit.)
Presentation: White Powder
Format: Powder
NOTES: Inhibitors: The enzyme is inhibited by heavy metals, the natural trypsin inhibitors to various degrees, an inhibitor from potato, and organophosphorus compounds. Also inhibited by AEBSF, α-1-antitrypsin, Aprotinin, DFP, PMSF, TPCK and α-2-Macroglobulin.
Storage & Handling: +4°C