α-Chymotrypsin from bovine pancreas
SIGMA/C3142 - (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein
Synonym: TLCK-Chymotrypsin
CAS Number: 9004-07-3
EC Number: 232-671-2
MDL Number: MFCD00130481
Product Type: Chemical
| form | essentially salt-free, lyophilized powder |
| mol wt | 25 kDa |
| Quality Level | 200 ![]() |
| solubility | 1 mM HCl: soluble 10 mg/mL, clear |
| specific activity | ≥40 units/mg protein |
| storage temp. | −20°C |
| type | Type VII |
| UniProt accession no. | P00767 ![]() |
| Analysis Note: | Protein determined by A |
| Application: | α-Chymotrypsin from Sigma 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. |
| 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. 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+. |
| 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. |
| Other Notes: | One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C. |
| Other Notes: | View more information on chymotrypsin at www.sigma-aldrich.com/enz![]() |
| Packaging: | 10, 25, 100 mg in glass bottle |
| Preparation Note: | TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity. |
| Symbol | ![]() ![]() GHS07,GHS08,GHS09 |
| Signal word | Danger |
| Hazard statements | H302 - H315 - H319 - H334 - H335 - H400 |
| Precautionary statements | P261 - P273 - P301 + P312 - P302 + P352 - P304 + P340 + P312 - P305 + P351 + P338 |
| Hazard Codes | Xn |
| Risk Statements | 36/37/38-42 |
| Safety Statements | 22-24-26-36/37 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| activity | specific activity: ≥40 units/mg protein |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.4.21.1 ( BRENDA ![]() ![]() |
| UNSPSC | 12352204 |




