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C9268

Sigma-Aldrich

Carboxypeptidase A from bovine pancreas

(Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution

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Synonym(s):
Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
CAS Number:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

grade

Proteomics Grade

form

ready-to-use solution

quality

(Type II-PMSF treated)

specific activity

≥50 units/mg protein

mol wt

~35 kDa

purified by

2× crystallization

impurities

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

storage temp.

2-8°C

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This Item
SAE0046C9584C1261
vibrant-m

C1261

Carboxypeptidase A−Agarose

specific activity

≥50 units/mg protein

specific activity

≥20 units/mg protein

specific activity

≥125 units/mg protein

specific activity

≥6 units/mL packed gel, 25 °C

impurities

≤0.05 BTEE units/mg protein chymotrypsin, ≤10 BAEE units/mg protein trypsin

impurities

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

impurities

-

impurities

-

form

ready-to-use solution

form

aqueous suspension

form

lyophilized powder

form

ammonium sulfate suspension

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

mol wt

~35 kDa

mol wt

~35 kDa

mol wt

34,000 Da± 600

mol wt

~35,250

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.
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 α-tubulin, in vitro, in order to induce high affinity to ethyl-N-phenylcarbamate (EPC) sepharose.

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.

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

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter


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Protocols

To measure carboxypeptidase A activity, hippuryl-L-phenylalanine is used in a continuous spectrophotometric rate determination assay at 254 nm. Carboxypeptidase A hydrolyzes peptide bonds at C-terminal residues.

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