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C1261

Sigma-Aldrich

Carboxypeptidase A−Agarose

ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, enzyme from bovine pancreas

Synonym(s):

Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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About This Item

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

enzyme from bovine pancreas

Quality Level

form

ammonium sulfate suspension

specific activity

≥6 units/mL packed gel, 25 °C

mol wt

~35,250

matrix

beaded agarose

storage temp.

2-8°C

General description

Carboxypeptidase A-agarose product is prepared by the immobilization of carboxypeptidase A, originally isolated from the bovine pancreas, to activated 4% crosslinked beaded agarose.

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.
Carboxypeptidase A is attached covalently to agarose or aldehyde and is effective for immobilization studies.

Unit Definition

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

Physical form

Suspension in 2.0 M (NH4)2SO4, pH 7

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

EU REACH Annex XVII (Restriction List)

CAS No.

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Deleting Mcl-1 in mast cells: getting 2 birds with 1 stone.
Booki Min
Blood, 118(26), 6729-6730 (2011-12-24)
Brian P Austin et al.
Protein expression and purification, 82(1), 116-124 (2011-12-27)
The carboxypeptidase A enzyme from Metarhizium anisopliae (MeCPA) has broader specificity than the mammalian A-type carboxypeptidases, making it a more useful reagent for the removal of short affinity tags and disordered residues from the C-termini of recombinant proteins. When secreted
Günter Wulff et al.
Accounts of chemical research, 45(2), 239-247 (2011-10-05)
The impressive efficiency and selectivity of biological catalysts has engendered a long-standing effort to understand the details of enzyme action. It is widely accepted that enzymes accelerate reactions through their steric and electronic complementarity to the reactants in the rate-determining
Beat Amrein et al.
Metallomics : integrated biometal science, 4(4), 379-388 (2012-03-07)
Among natural metalloenzymes, the facial two-histidines one-carboxylate binding motif (FTM) is a widely represented first coordination sphere motif present in the active site of a variety of metalloenzymes. A PDB search revealed a total of 1685 structures bearing such FTMs
Arthur A Topilow et al.
Cancer biomarkers : section A of Disease markers, 10(1), 27-33 (2012-02-03)
Pancreatic cancer has a dismal prognosis because it is often diagnosed at an advanced stage. Therefore, serological biomarkers are eagerly sought for early detection. The digestive enzyme pro-carboxypeptidase A (PCPA) may be able to fill this role. The purpose of

Protocols

Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.

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