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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:
9035-75-0
EC Number:
232-905-3
MDL number:
MFCD00130483
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

200

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.

P00767

foreign activity

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

storage temp.

−20°C

Gene Information

cow ... CTRB1(618826)

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

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Curtiss P Schneider et al.
The journal of physical chemistry. B, 115(22), 7447-7458 (2011-05-17)
L-Arginine hydrochloride is a very important aggregation suppressor for which there has been much attention given regarding elucidating its mechanism of action. Little consideration, however, has been given toward other salt forms besides chloride, even though the counterion likely imparts
Curtiss P Schneider et al.
The journal of physical chemistry. B, 113(7), 2050-2058 (2009-02-10)
The relatively new technique of vapor pressure osmometry was utilized to determine the preferential interaction of five common solution additives (arginine HCl, guanidine HCl, glycerol, glucose, and urea) using three different model proteins (BSA, lysozyme, and alpha-chymotrypsinogen). Results for guanidine
Effect of real-world sounds on protein crystallization
Zhang CY, et al.
International Journal of Biological Macromolecules, 112, 841-851 (2018)
Pedro P Madeira et al.
Journal of chromatography. A, 1190(1-2), 39-43 (2008-04-02)
Distribution coefficients of randomly selected proteins were measured in aqueous two-phase systems (ATPSs) formed by different combinations of Dextran-75 (Dex), Ficoll-70, polyethylene glycol-8000 (PEG), hydroxypropyl starch-100 (PES), and Ucon50HB5100 (Ucon, a random copolymer of ethylene glycol and propylene glycol) at
Shujun Bai et al.
Journal of pharmaceutical sciences, 94(9), 2030-2038 (2005-07-30)
Fourier transform infrared (FTIR) spectroscopy is a powerful tool for monitoring structural changes in lyophilized protein formulations. However, direct measurement of IR spectra requires significant handling time and effort. The possibility of using near infrared (NIR) spectroscopy as a rapid
View All Related Papers

Articles

HPLC Analysis of Proteins on TSKgel® BioAssist S

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX-NP5: Affect of pH

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX: Affect of Particle Size

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

Chymotrypsin

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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