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Key Documents

C7762

Sigma-Aldrich

α-Chymotrypsin from bovine pancreas

Type I-S, essentially salt-free, lyophilized powder

Synonyme(s) :

α-chymotrypsin A and B, alpha-chymotrypsin

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
eCl@ss :
42010112
Nomenclature NACRES :
NA.54

Type

Type I-S

Niveau de qualité

Forme

essentially salt-free, lyophilized powder

Activité spécifique

≥40 units/mg protein

Poids mol.

25 kDa

Produit purifié par

3× crystallization

Solubilité

1 mM HCl: soluble 2.0 mg/mL, clear

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

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Application

α-Chymotrypsin from bovine pancreas has been used in a study to investigate protein extraction by Winsor-III microemulsion systems. α-Chymotrypsin from bovine pancreas has also been used in a study to investigate a new specific fullerene-based fluorescent probe for trypsin.
The product has been used to investigate the inhibitory effect of several ether oligomers against the enzyme. It has also been used to cleave pro-phenoloxidase in order to estimate total phenoloxidase in haemolymph. Furthermore, the enzyme has been used as a positive control in chymotrypsin assays using salivary gland and anterior midgut extracts of Deraeocoris nigritulus.

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, as well as 10 mM of 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

Prepared free of autolysis products and low molecular weight contaminants.
The powder may be reconstituted in 1 mM HCl at 2 mg/mL concentration to form a clear solution.

Remarque sur l'analyse

Minimum 85% protein
Protein determined by E1%/280

Autres remarques

Pictogrammes

Health hazardExclamation markEnvironment

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)

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Consulter la Bibliothèque de documents

Nathan W Bailey et al.
Biology letters, 7(2), 217-220 (2010-09-03)
Increased investment in immunity is expected to be beneficial under crowded conditions because of the greater risk of pathogen and parasite transmission, but the evolution of this facultative response relies on the ability to accurately assess social cues in the
Olivier Renaudet et al.
Organic letters, 6(3), 397-400 (2004-01-30)
[structure: see text] Hydroxyaromatic aldehydes and ketones were used as building blocks to prepare ether oligomers. An iterative two-step protocol involving Mitsunobu coupling and carbonyl reduction provided a protecting-group-free route with high yields. Activity screening of an 84-member library against
Lakshmi Swarnalatha Jasti et al.
Biotechnology progress, 30(2), 317-323 (2014-01-23)
Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel
S J Perkins et al.
The Biochemical journal, 295 ( Pt 1), 87-99 (1993-10-01)
Solution scattering is a powerful means of determining the overall arrangement of domains in the multidomain proteins of complement. the serine-proteinase domain is central to all proteolytic events during complement activation. As models of this domain, bovine beta-trypsin, trypsinogen, alpha-chymotrypsin
J A Hodgson et al.
Journal of general microbiology, 131(12), 3219-3227 (1985-12-01)
The effects of elevated temperature and of digestion with a variety of proteinases on the flocforming ability of flocculent strains of Saccharomyces cerevisiae, both genetically defined (FLO1 and FLO5) laboratory and genetically undefined brewing strains, have been determined. This has

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