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C6423

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

suitable for protein sequencing, salt-free, lyophilized powder

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42010112
NACRES:
NA.26

grade

Proteomics Grade

Quality Level

form

salt-free, lyophilized powder

mol wt

25 kDa

suitability

suitable for protein sequencing

UniProt accession no.

storage temp.

2-8°C

Gene Information

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This Item
C8946C7762C4129
form

salt-free, lyophilized powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

lyophilized powder

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

mol wt

25 kDa

suitability

suitable for protein sequencing

suitability

-

suitability

-

suitability

-

UniProt accession no.

P00767

UniProt accession no.

P17538

UniProt accession no.

P00767

UniProt accession no.

P00767

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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

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

Certificates of Analysis (COA)

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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
The α-chymotrypsin-catalyzed Povarov reaction: one-pot synthesis of tetrahydroquinoline derivatives.
Li LP, et al.
Green Chemistry, 17(5), 3148-3156 (2015)
Methods in molecular biology. v. 16
Burrell, MM
BioChemistry: An Indian Journal (1993)
Johnston et al.
The Journal of experimental biology, 201 (Pt 12), 623-646 (1998-02-06)
The influence of embryonic and larval temperature regime on muscle growth was investigated in Atlantic herring (Clupea harengus L.). Eggs of spring-spawning Clyde herring were incubated at 5 degrees C, 8 degrees C or 12 degrees C until hatching and
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

Articles

Chymotrypsin

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

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