Product Name

α-Chymotrypsin from bovine pancreas

Synonym

TLCK-Chymotrypsin

Assay

TLCK treated to inactivate residual tryspin activity, Type VII, essentially salt-free, ≥40 units/mg protein

CAS Number

9004-07-3

MDL number

MFCD00130481

Molecular Weight

mol wt 25 kDa

Suitability

BioReagent

l Physical and Chemical Information

Appearance

lyophilized powder

Solubility(25°C)

1 mM HCl: soluble 10 mg/mL, clear

l Biological Information

Biochem/Physiol Actions

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.

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) ed 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₊.

Application

α-Chymotrypsin 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.

Preparation Note

TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.

Unit Definition

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

l Storage

Storage temp.

-20°C

l Precautions and Disclaimer

This product is for R&D use only, not for drug, household, or other uses.

l References

1. http://www.drugbank.ca

2. https://ncit.nci.nih.gov

3. https://www.ncbi.nlm.nih.gov