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SAE0046

Sigma-Aldrich

Carboxypeptidase A from bovine pancreas

(Type II-PMSF treated), ≥20 units/mg protein

Synonyme(s) :

Carboxypeptidase A, Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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About This Item

Numéro CAS:
11075-17-5
Numéro de classification (Commission des enzymes):
3.4.17.1 (BRENDA, IUBMB)
Numéro MDL:
MFCD00130718
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bovine pancreas

Niveau de qualité

200

Forme

aqueous suspension

Qualité

(Type II-PMSF treated)

Activité spécifique

≥20 units/mg protein

Poids mol.

~35 kDa

Produit purifié par

2× crystallization

Impuretés

≤0.05 BTEE units/mg protein chymotrpsin
≤10 BAEE units/mg protein trypsin

Température de stockage

2-8°C

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Description générale

Carboxypeptidase A (CPA) is a secreted protease is liberated after the activation of mast cells to facilitate acute anaphylaxis. Carboxypeptidase A has a long half-life in vivo, when compared to other secreted proteases.

Application

Carboxypeptidase A from bovine pancreas has been used in in vitro simulated digestion.
Carboxypeptidase A from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase A in Escherichia coli. Carboxypeptidase A from bovine pancreas has also been used in a study to investigate the isolation and partial characterization of precursor forms of ostrich carboxypeptidase.

Actions biochimiques/physiologiques

Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by β-phenylpropionate and indole acetate.†

Définition de l'unité

One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.

Notes préparatoires

Treated with phenylmethylsulfonyl fluoride to eliminate trypsin and chymotrypsin activity. Dialyzed and recrystallized: aqueous suspension with toluene added.

Remarque sur l'analyse

Protein determined by E1%/278

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Quantification of Multifunctional Dipeptide YA from Oyster Hydrolysate for Quality Control and Efficacy Evaluation
Xie C L, et al.
BioMed Research International, 2018, 13288-13288 (2018)
The role of zinc in carboxypeptidase.
Bert Vallee
The Journal of Biological Chemistry, 235.1, 64-69 (1960)
Mast cell tryptase and carboxypeptidase A expression in body fluid and gastrointestinal tract associated with drug-related fatal anaphylaxis
Guo X J, et al.
World Journal of Gastroenterology, 21(47), 13288-13288 (2015)
Cheng-Liang Xie et al.
BioMed research international, 2018, 8437379-8437379 (2018-10-23)
YA is an angiotensin-I-converting enzyme- (ACE-) inhibitory peptide from oyster hydrolysate with antihypertensive activity. Its antioxidant and anti-inflammatory activity were investigated in this study. YA can dose-dependently quench DPPH and ABTS radical and inhibit lipopolysaccharide-induced nitric oxide in RAW 264.7

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