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SAE0046

Sigma-Aldrich

Carboxypeptidase A from bovine pancreas

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

Sinônimo(s):

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

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About This Item

Número CAS:
11075-17-5
Número da licença da enzima:
3.4.17.1 (BRENDA, IUBMB)
Número MDL:
MFCD00130718
Código UNSPSC:
12352204
NACRES:
NA.54

fonte biológica

bovine pancreas

Nível de qualidade

200

Formulário

aqueous suspension

qualidade

(Type II-PMSF treated)

atividade específica

≥20 units/mg protein

peso molecular

~35 kDa

purificado por

2× crystallization

Impurezas

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

temperatura de armazenamento

2-8°C

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Descrição geral

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.

Aplicação

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.

Ações bioquímicas/fisiológicas

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.†

Definição da unidade

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

Nota de preparo

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

Nota de análise

Protein determined by E1%/278

Pictogramas

Health hazard
GHS08

Palavra indicadora

Danger

Frases de perigo

H334

Classificações de perigo

Resp. Sens. 1

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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Certificados de análise (COA)

Lot/Batch Number
SLBQ7226V

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Visite a Biblioteca de Documentos

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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