C7762
α-Chymotrypsin from bovine pancreas
Type I-S, essentially salt-free, lyophilized powder
Synonym(s):
α-chymotrypsin A and B, alpha-chymotrypsin
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About This Item
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type
Type I-S
Quality Level
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
cow ... CTRB1(618826)
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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.
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
View more information on chymotrypsin at www.sigma-aldrich.com/enzymeexplorer
inhibitor
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
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
Certificates of Analysis (COA)
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Articles
Analytical Enzyme Chymotrypsin: Chymotrypsin is produced in the acinar cells of the pancreas as the inactive precursor, chymotrypsinogen.
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