Carboxypeptidase A from bovine pancreas, (Type II-PMSF treated), >=50 units/mg protein, aqueous susp

Stock Code: 3579302
Manufacturer Part No: C9268-2.5KU
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Analysis Note


Protein determined by E1%/278


Application


The enzyme from Sigma has been used as a comparison to study the specificity of Metarhizium anisopliae carboxypeptidase A (MeCPA). MeCPA had been genetically engineered to facilitate the removal of polyhistidine tags from the C-termini of recombinant proteins. It has also been used to de-tyrosinate ?-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.


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 beta-phenylpropionate and indole acetate.


Packaging


500, 2500, 5000 units in glass bottle


Preparation Note


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


Unit Definition


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

Quality Level300
ManufacturerSIGMA-ALDRICH
Storage Temp.2-8°C
Impurities≤0.05 BTEE units/mg protein chymotrypsin, ≤10 BAEE units/mg protein trypsin
Formaqueous suspension

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