SAE0046

Carboxypeptidase A

Cleaves C-terminal amino acids, suitable for Mass Spectrometry, from bovine pancreas

• Synonym(e): Carboxypolypeptidase, Peptidyl-L-aminosäure-Hydrolase
• CAS-Nummer: 11075-17-5
• UNSPSC Code: 12352204
• NACRES: NA.54
• EG-Nummer: 3.4.17.1 (BRENDA, IUBMB)
• MDL number: MFCD00130718
• Specific activity: ≥20 units/mg protein
• Biological source: bovine pancreas

Eigenschaften

• Produktname: Carboxypeptidase A aus Rinderpankreas, (Type II-PMSF treated), ≥20 units/mg protein
• biological source: bovine pancreas
• Quality Segment: 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

Beschreibung

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 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.

Carboxypeptidase A from bovine pancreas has been used in in vitro simulated digestion.

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.†

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

Other Notes

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

Sicherheitshinweise

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• Hazard Classifications: Resp. Sens. 1
• Lagerklasse: 10 - Combustible liquids
• wgk: WGK 2
• flash_point_f: Not applicable
• flash_point_c: Not applicable