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C4879

Sigma-Aldrich

α-Chymotrypsinogen A from bovine pancreas

essentially salt-free, lyophilized powder

Synonyme(s) :

chymotrypsin A zymogen

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About This Item

Numéro CAS:
9035-75-0
Numéro CE :
232-905-3
Numéro MDL:
MFCD00130483
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bovine pancreas

Niveau de qualité

200

Type

Type II

Forme

essentially salt-free, lyophilized powder

Activité spécifique

≥40 units/mg solid

Poids mol.

25,656 Da by calculation

Produit purifié par

6× crystallization

Solubilité

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

Numéro d'accès UniProt

P00767

Activité étrangère

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

Température de stockage

−20°C

Informations sur le gène

cow ... CTRB1(618826)

Catégories apparentées

Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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

Autres remarques

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
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
Structural basis of IgE binding to alpha-and gamma-gliadins: Contribution of disulfide bonds and repetitive and nonrepetitive domains
Mameri H, et al.
Journal of Agricultural and Food Chemistry, 63(29), 6546-6554 (2015)
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)
Afficher tous les articles scientifiques apparentés

Articles

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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