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α-Chymotrypsin from bovine pancreas

suitable for protein sequencing, salt-free, lyophilized powder

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About This Item

Número de CAS:
9004-07-3
Comisión internacional de enzimas:
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

signalword

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

11 - Combustible Solids

wgk_germany

WGK 1

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Certificados de análisis (COA)

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Tessa E F Quax et al.
Virology, 404(1), 1-4 (2010-05-22)
Recently a unique mechanism of virion release was discovered in Archaea, different from lysis and egress systems of bacterial and eukaryotic viruses. It involves formation of pyramidal structures on the host cell surface that rupture the S-layer and by opening
A new platform for chymotrypsin isolation from fresh bovine pancreas using an environmental friendly polyelectrolyte: Alginate
Rausch C, et al.
BioChemistry: An Indian Journal, 9(6), 213-220 (2015)
L M Simon et al.
Biochemical and biophysical research communications, 280(5), 1367-1371 (2001-02-13)
The effects of different concentrations (20-95%) of organic solvents (ethanol, 1,4-dioxane and acetonitrile) were studied on alpha-chymotrypsin and trypsin from bovine pancreas. The changes in secondary structure were followed by CD measurements, and the apparent Michaelis constants (KMapp) and the
S Herrero et al.
Applied and environmental microbiology, 67(3), 1085-1089 (2001-03-07)
Susceptibility to protoxin and toxin forms of Cry1Ab and the binding of (125)I-labeled Cry1Ab and Cry1Ac has been examined in three Plodia interpunctella colonies, one susceptible (688(s)) and two resistant (198(r) and Dpl(r)) to Bacillus thuringiensis. Toxicological studies showed that
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
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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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