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Safety Information

SAE0046

Sigma-Aldrich

Carboxypeptidase A from bovine pancreas

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

Synonym(s):

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

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About This Item

CAS Number:
11075-17-5
Enzyme Commission number:
3.4.17.1 (BRENDA, IUBMB)
MDL number:
MFCD00130718
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

200

form

aqueous suspension

quality

(Type II-PMSF treated)

specific activity

≥20 units/mg protein

mol wt

~35 kDa

purified by

2× crystallization

impurities

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

storage temp.

2-8°C

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General description

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.

Biochem/physiol Actions

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.†

Unit Definition

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

Preparation Note

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

Analysis Note

Protein determined by E1%/278

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Hazard Classifications

Resp. Sens. 1

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

动植物源性产品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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)
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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