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C6423

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

suitable for protein sequencing, salt-free, lyophilized powder

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About This Item

CAS Number:
9004-07-3
Enzyme Commission number:
3.4.21.1 (BRENDA, IUBMB)
EC Number:
232-671-2
MDL number:
MFCD00130481
UNSPSC Code:
12352204
eCl@ss:
42010112
NACRES:
NA.26

grade

Proteomics Grade

Quality Level

200

form

salt-free, lyophilized powder

mol wt

25 kDa

suitability

suitable for protein sequencing

UniProt accession no.

P00767

storage temp.

2-8°C

Gene Information

cow ... CTRB1(618826)

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General description

α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein. The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.
Chymotrypsin (Chy) is a serine protease. It corresponds to a molecular weight of 25.7 kDa and is widely used in pharmaceutical industry. It is synthesized in pancreas from chymotrypsinogen and require calcium for this conversion.

Application

α-Chymotrypsin from bovine pancreas is used for the following applications:
  • Protein Identification by mass spectrometry (MS)
  • The isolation and characterization of myosin heavy chains
  • Toxin preparation
  • The incubation of infected and uninfected cells for analysis of cellular proteins by SDS-PAGE
α-Chymotrypsin from bovine pancreas (BPC) may be used as a catalyst in the preparation of tetrahydroquinoline derivatives by Povarov reaction.

Biochem/physiol Actions

α-Chymotrypsin from bovine pancreas is stabilized by Ca2+ and catalyzes the hydrolysis of peptide bonds in particular the amino acids tyrosine, phenylalanine, tryptophan, and leucine at their C-terminal side. α-Chymotrypsin is inhibited by Cu2+ and Hg.
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.

Other Notes

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

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substrate

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Description
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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

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Xinyu Liu et al.
eLife, 9 (2020-12-05)
The production of reactive oxygen species (ROS) is a ubiquitous defense response in plants. Adapted pathogens evolved mechanisms to counteract the deleterious effects of host-derived ROS and promote infection. How plant pathogens regulate this elaborate response against ROS burst remains
The α-chymotrypsin-catalyzed Povarov reaction: one-pot synthesis of tetrahydroquinoline derivatives.
Li LP, et al.
Green Chemistry, 17(5), 3148-3156 (2015)
Miguel Ribeiro et al.
International journal of molecular sciences, 14(3), 5650-5667 (2013-03-13)
Analysis of Portuguese wheat (Triticum aestivum L.) landrace 'Barbela' revealed the existence of a new x-type high molecular weight-glutenin subunit (HMW-GS) encoded at the Glu-A1 locus, which we named 1Ax1.1. Using one-dimensional and two-dimensional electrophoresis and mass spectrometry, we compared
Samir Kumar Pal et al.
Proceedings of the National Academy of Sciences of the United States of America, 99(24), 15297-15302 (2002-11-13)
We report studies of hydration dynamics at the surface of the enzyme protein bovine pancreatic alpha-chymotrypsin. The probe is the well known 1-anilinonaphthalene-8-sulfonate, which binds selectively in the native state of the protein, not the molten globule, as shown by
Methods in molecular biology. v. 16
Burrell, MM
BioChemistry: An Indian Journal (1993)
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Chymotrypsin

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

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