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C7762 Sigma

α-Chymotrypsin from bovine pancreas

Type I-S, essentially salt-free, lyophilized powder

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Chymotrypsin, alpha-,
type   Type I-S
form   essentially salt-free, lyophilized powder
activity   ≥40 units/mg protein
mol wt   mol wt 25 kDa
purified by   3× crystallization
solubility   1 mM HCl: soluble2.0 mg/mL, clear
storage temp.   −20°C
Gene Information   cow ... CTRB1(618826)

Description

Frequently Asked Questions

Frequently Asked Questions are available for this Product.

Analysis Note

Minimum 85% protein

Protein determined by E1%/280

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) 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, as well as 10 mM of Cu2+ and Hg2+.

Other Notes

View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer

Packaging

5, 25, 100 mg in glass bottle

Preparation Note

Prepared free of autolysis products and low molecular weight contaminants.

The powder may be reconstituted in 1 mM HCl at 2 mg/mL concentration to form a clear solution.

Unit Definition

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

Application

α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin.

The product has been used to investigate the inhibitory effect of several ether oligomers against the enzyme. It has also been used to cleave pro-phenoloxidase in order to estimate total phenoloxidase in haemolymph. Furthermore, the enzyme has been used as a positive control in chymotrypsin assays using salivary gland and anterior midgut extracts of Deraeocoris nigritulus.

Price and Availability

Suggested Laboratory Gloves


Laboratory GlovesThis substance has been tested against several types of hand protection for CE compliance. Click below to find the recommended gloves for handling this product.



Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
GC3050000
Protocols & Articles

Protocols

Procedure for Enzymatic Assay of Chymotrypsin (α‑Chymotrypsin, EC 3.4.21.1)

This procedure is for products with a specification for Chymotrypsin activity. It is not to be used to assay Insoluble Chymotrypsin such as Catalog No. C9134. The procedure is a continuous spectropho...
Keywords: Extinction coefficient

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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