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C4129

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

Type II, lyophilized powder, ≥40 units/mg protein

Synonyme(s) :

α-chymotrypsin A and B, alpha-chymotrypsin

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About This Item

Numéro CAS:
9004-07-3
Numéro de classification (Commission des enzymes):
3.4.21.1 (BRENDA, IUBMB)
Numéro CE :
232-671-2
Numéro MDL:
MFCD00130481
Code UNSPSC :
12352204
eCl@ss :
42010112
Nomenclature NACRES :
NA.54

Type

Type II

Niveau de qualité

300

Forme

lyophilized powder

Activité spécifique

≥40 units/mg protein

Poids mol.

25 kDa

Composition

protein, ≥85%

Couleur

white to off-white

Numéro d'accès UniProt

P00767

Application(s)

diagnostic assay manufacturing

Température de stockage

−20°C

Informations sur le gène

cow ... CTRB1(618826)

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Catégories apparentées

Application

The enzyme from Sigma has been used to study the structure-function relationship in glycosylated α-chymotrypsin using immobilized metal-ion affinity chromatography (IMAC) and immobilized metal-ion affinity capillary electrophoresis (IMACE).

Actions biochimiques/physiologiques

α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. The pI is 8.75. It selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca2+ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10 mM Cu2+ and Hg2+.
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.

Définition de l'unité

One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.

Notes préparatoires

Produced from 3× crystallized chymotrypsinogen

Remarque sur l'analyse

Protein determined by E1%/280

Autres remarques

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

Application

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Description
Tarif

Inhibiteur

Réf. du produit
Description
Tarif

A2504

6-Aminocaproic acid, ≥99% (titration), powder

A7824

6-Aminocaproic acid, BioUltra, ≥99%

D0879

Diisopropylfluorophosphate

L2023

Leupeptin trifluoroacetate salt, ≥90% (HPLC), microbial

T9777

Trypsin-chymotrypsin inhibitor from Glycine max (soybean), lyophilized powder

A1153

Aprotinine from bovine lung, lyophilized powder, 3-8 TIU/mg solid

P7626

Fluorure de phénylméthanesulfonyle, ≥98.5% (GC)

B1552

Bromoenol lactone, ≥98% (TLC)

A9024

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A6150

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A9285

α1-Antichymotrypsin from human plasma, ≥92.5% (SDS-PAGE), lyophilized powder

T4376

N-p-Tosyl-L-phénylalanine chlorométhyl cétone, ≥97% (TLC), powder

C7268

Chymostatin, microbial

Substrat

Réf. du produit
Description
Tarif

Pictogrammes

Health hazardExclamation markEnvironment
GHS08,GHS07,GHS09

Mention d'avertissement

Danger

Classification des risques

Acute Tox. 4 Oral - Aquatic Acute 1 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Équipement de protection individuelle

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

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Certificats d'analyse (COA)

Lot/Batch Number
SLCH1926
SLBV2540
SLBT5554
SLBG2821V
010M7019V

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Antonio Jesús Vizcaíno et al.
Marine drugs, 18(6) (2020-06-24)
This piece of research evaluates the presence of protease inhibitors in the macroalga Ulva ohnoi and provides an initial overview of their mode of action. The ability of Ulva protease inhibitors to inhibit digestive proteases of three marine fish species
Xiaojing Du et al.
Journal of the science of food and agriculture, 98(8), 3140-3147 (2017-12-08)
To investigate the change of bioavailability and structure of myofibrillar proteins during Nanjing dry-cured duck processing, carbonyl content, sulfhydryl (SH) group, disulfide (SS) group, sodium dodecyl sulfate polyacrylamide gel electrophoresis, surface hydrophobicity, secondary structures and in vitro digestibility were determined.
Ines Atuh Ngoh et al.
Experimental parasitology, 218, 107969-107969 (2020-08-29)
Invasion of human red blood cells (RBCs) by Plasmodium parasites is a crucial yet poorly characterised phenotype. Two-color flow cytometry (2cFCM) promises to be a very sensitive and high throughput method for phenotyping parasite invasion. However, current protocols require high
Shannon Gwala et al.
Food & function, 11(3), 2509-2521 (2020-03-07)
Postharvest storage of legumes is a strategy to ensure food security. However, the hard-to-cook phenomenon, partly explained by pectin-cation-phytate theory, may develop during storage. Based on this theory, minerals could be redistributed within the matrix, affecting the concentration of free/bound
Robert Winkler
Rapid communications in mass spectrometry : RCM, 24(3), 285-294 (2010-01-06)
Electrospray ionization (ESI) ion trap mass spectrometers with relatively low resolution are frequently used for the analysis of natural products and peptides. Although ESI spectra of multiply charged protein molecules also can be measured on this type of devices, only
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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