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C3142

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

(TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein

Synonyme(s) :

TLCK-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 VII

Forme

essentially salt-free, lyophilized powder

Activité spécifique

≥40 units/mg protein

Poids mol.

25 kDa

Solubilité

1 mM HCl: soluble 10 mg/mL, clear

Numéro d'accès UniProt

P00767

Température de stockage

−20°C

Informations sur le gène

cow ... CTRB1(618826)

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Catégories apparentées

Application

α-Chymotrypsin from Sigma has been used to determine the crystal structures of two homologous inhibitors (pars intercerebralis major peptide-C and pars intercerebralis major peptide-D2v) from the insect Locusta migratoria by forming a complex with the enzyme.

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. Its 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, 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

TLCK treatment inactivates trypsin which may be present in chymotrypsin, without affecting the chymotrypsin activity.

Remarque sur l'analyse

Protein determined by A1%/280

Autres remarques

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

Inhibiteur

Réf. du produit
Description
Tarif

A2504

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

A7824

6-Aminocaproic acid, ≥99%, BioUltra

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

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

M Gestin et al.
Digestive diseases and sciences, 42(6), 1302-1311 (1997-06-01)
A specific method for pancreatic elastase II activity analysis was developed. True elastase II activity could be discriminated from that of elastase I and chymotrypsin. The postnatal development of four pancreatic proteases in the duodenal juice of children and in
Tommi Kotila et al.
Nature communications, 13(1), 3442-3442 (2022-06-16)
Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the 'ancient' actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same
A Roussel et al.
The Journal of biological chemistry, 276(42), 38893-38898 (2001-08-10)
The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine alpha-chymotrypsin at 2.1- and 3.0-A resolution, respectively. PMP-C is a potent bovine alpha-chymotrypsin inhibitor whereas native PMP-D2 is
Tobias Koschubs et al.
Nucleic acids research, 38(10), 3186-3195 (2010-02-04)
Mediator is the central coactivator complex required for regulated transcription by RNA polymerase (Pol) II. Mediator consists of 25 subunits arranged in the head, middle, tail and kinase modules. Structural and functional studies of Mediator are limited by the availability
Zhenyao Luo et al.
FEBS letters, 592(13), 2341-2350 (2018-06-02)
The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn2+ for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn2+ homeostasis. However, the mechanistic basis
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.

Protocoles

Procedure for Enzymatic Assay of α-Chymotrypsin (EC 3.4.21.1)

Follow our procedure for the determination of a chymotrypsin activity. This enzymatic assay of alpha chymotrypsin guides you through the entire process and necessary calculations.

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