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Merck

C1261

Sigma-Aldrich

Carboxypeptidase A−Agarose

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

Sinónimos:

Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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About This Item

Comisión internacional de enzimas:
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

substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Stabilization-immobilization of carboxypeptidase A to aldehyde-agarose gels: A practical example in the hydrolysis of casein
Pedroche J, et al.
Enzyme and Microbial Technology, 711-718 null
Deleting Mcl-1 in mast cells: getting 2 birds with 1 stone.
Booki Min
Blood, 118(26), 6729-6730 (2011-12-24)
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
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
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

Protocolos

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

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

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

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

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