Merck
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C7762

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

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

Synonym(s):
alpha-chymotrypsin, α-chymotrypsin A and B
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42010112
NACRES:
NA.54

Quality Level

type

Type I-S

form

essentially salt-free, lyophilized powder

specific activity

≥40 units/mg protein

mol wt

25 kDa

purified by

3× crystallization

solubility

1 mM HCl: soluble 2.0 mg/mL, clear

UniProt accession no.

storage temp.

−20°C

Gene Information

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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.

Packaging

5, 25, 100 mg in glass bottle

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. 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+.
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.

Unit Definition

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

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.

Analysis Note

Minimum 85% protein
Protein determined by E1%/280

Other Notes

Signal Word

Danger

Hazard Classifications

Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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Product Information Sheet

More Documents

Quotes and Ordering

Articles

Chymotrypsin

Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.

Protocols

Procedure for Enzymatic Assay of α-Chymotrypsin (EC 3.4.21.1)

Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.

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