SAE0046
Carboxypeptidase A
Cleaves C-terminal amino acids, suitable for Mass Spectrometry, from bovine pancreas
Synonym(s):
Carboxypeptidase A, Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥20 units/mg protein
Biological source:
bovine pancreas
Product Name
Carboxypeptidase A from bovine pancreas, (Type II-PMSF treated), ≥20 units/mg protein
biological source
bovine pancreas
Quality Segment
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
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.
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.