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C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Synonym(s):

chymotrypsin A zymogen

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

type

Type II

form

essentially salt-free, lyophilized powder

specific activity

≥40 units/mg solid

mol wt

25,656 Da by calculation

purified by

6× crystallization

solubility

1 mM HCl: soluble 10 mg/mL, clear, colorless

UniProt accession no.

foreign activity

α-chymotrypsin ≤1 U/mg (prior to activation by trypsin)

storage temp.

−20°C

Gene Information

Related Categories

General description

Chymotrypsinogen from bovine pancreas is a zymogen containing 5 disulfide bridges. It has an isoelectric pH of 8.97.

Application

α-Chymotrypsinogen A from bovine pancreas has been used as model protein crystallization reproducibility studies. It has also been used in the hydrolysis of α-gliadins prior to mass spectroscopy studies.
The enzyme from Sigma has been used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy. It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. The enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. In this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution.

Biochem/physiol Actions

Chymotrypsinogen A requires limited proteolysis for its activation. Chymotrypsinogen A may be activated by trypsin and chymotrypsin (autolytic activation) to form m α, β, γ, δ and π chymotrypsin (depending upon the conditions of activation). Chymotrypsin is a protease that will preferentially cleave peptides on the carboxyl side of aromatic amino acids including tryptophan, tyrosine, and phenylalanine. It will also hydrolyze peptides on the carboxyl side of leucine, methionine, and alanine.
A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond.

Unit Definition

After activation to Chymotrypsin, one unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Other Notes

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品

Certificates of Analysis (COA)

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Simulation of the activation of alpha-chymotrypsin: Analysis of the pathway and role of the propeptide
Matrai J, et al.
Protein Science, 13(12), 3139-3150 (2004)
Rob Haselberg et al.
Analytica chimica acta, 678(1), 128-134 (2010-09-28)
A capillary electrophoresis-mass spectrometry (CE-MS) method using sheath liquid electrospray ionization interfacing was studied and optimized for the analysis of intact basic proteins. To prevent protein adsorption, capillaries with a noncovalent positively charged coating were utilized. Capillaries were coated by
9.1 Proteases: Facilitating a Difficult Reaction
Biochemistry (5th Edition) (2002)
Peter M Tessier et al.
Biophysical journal, 82(3), 1620-1631 (2002-02-28)
Weak protein interactions are often characterized in terms of the osmotic second virial coefficient (B(22)), which has been shown to correlate with protein phase behavior, such as crystallization. Traditional methods for measuring B(22), such as static light scattering, are too
On the activation of bovine chymotrypsinogen A. Conformational isomerization of alpha1-and kappa-chymotrypsin and their autolytic conversion to alpha-and gamma-chymotrypsin.
Sharma SK and Hopkins TR
The Journal of Biological Chemistry, 253(9), 3055-3061 (1978)

Articles

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

Chromatograms

application for HPLC

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