Product Name

α-Chymotrypsin−Agarose from bovine pancreas

Assay

2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)

Molecular Weight

mol wt 25 kDa

MDL number

MFCD00130481

Suitability

BioReagent

l Physical and Chemical Information

Appearance

White lyophilized powder

Physical form

Stabilized with lactose

l Biological Information

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) ed 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₊.

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.

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.

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