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C9134

Sigma-Aldrich

α-Chymotrypsin−Agarose from bovine pancreas

lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)

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About This Item

Numéro de classification (Commission des enzymes):
3.4.21.1 (BRENDA, IUBMB)
Numéro MDL:
MFCD00130481
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bovine pancreas

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)

Poids mol.

25 kDa

Numéro d'accès UniProt

P00767

Température de stockage

−20°C

Informations sur le gène

cow ... CTRB1(618826)

Catégories apparentées

Application

α-Chymotrypsin agarose from bovine pancreas has been used to study the purification and characterization of glucoamylase. α-Chymotrypsin agarose from bovine pancreas has also been used in a study to investigate molecular modeling for the design of a biomimetic chimeric ligand.

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+.
Serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the bond.

Définition de l'unité

One unit will hydrolyze 1.0 μmole of N-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 8.0 at 30 °C.

Forme physique

Stabilized with lactose

Remarque sur l'analyse

Protein determined by A1%/280

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 mark
GHS08,GHS07

Mention d'avertissement

Danger

Mentions de danger

H315,H317,H319,H334,H335

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Équipement de protection individuelle

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

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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Saleh A Mohamed et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 140(1), 73-80 (2004-12-29)
The present study analyzed the existence of carbohydrases in camel pancreas compared to some other ruminants. Disaccharidases (maltase, cellobiase, lactase, trehalase and sucrase), glucoamylase and alpha-amylase were detected in pancreas of camel, sheep, cow and buffalo. Enzyme levels in sheep
Ke Xu et al.
The Journal of biological chemistry, 283(49), 34337-34344 (2008-10-11)
The clinical severity of Osteogenesis Imperfecta (OI), also known as the brittle bone disease, relates to the extent of conformational changes in the collagen triple helix induced by Gly substitution mutations. The lingering question is why Gly substitutions at different
N E Labrou et al.
Biotechnology and bioengineering, 63(3), 322-332 (1999-04-01)
Molecular modeling was employed for the design of a biomimetic chimeric ligand for L-lactate dehydrogenase (LDH). This ligand is an anthraquinone monochlorotriazinyl dye comprising two moieties: (a) the ketocarboxyl biomimetic moiety, 2-(4-aminophenyl)-ethyloxamic acid, linked on the monochlorotriazine ring, mimicking the
Y Gao et al.
The Journal of biological chemistry, 276(13), 9838-9845 (2001-01-20)
Dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine (O-GlcNAc) on Ser/Thr residues is ubiquitous in higher eukaryotes and is analogous to protein phosphorylation. The enzyme for the addition of this modification, O-GlcNAc transferase, has been cloned from several
Vincent Dechavanne et al.
Protein expression and purification, 87(2), 100-110 (2012-11-14)
The proteasome is a multicatalytic protease complex present in all eukaryotic cells, which plays a critical role in regulating essential cellular processes. During the immune response to pathogens, stimulation by γ interferon induces the production of a special form of
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.

Chymotrypsin

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

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