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C1261

Sigma-Aldrich

Carboxypeptidase A−Agarose

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

Synonyme(s) :

Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

enzyme from bovine pancreas

Niveau de qualité

Forme

ammonium sulfate suspension

Activité spécifique

≥6 units/mL packed gel, 25 °C

Poids mol.

~35,250

Matrice

beaded agarose

Température de stockage

2-8°C

Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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

Forme physique

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

Pictogrammes

Health hazardExclamation mark

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

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

Organes cibles

Respiratory system

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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
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
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
Zhenhua Li et al.
BMC bioinformatics, 13, 51-51 (2012-03-29)
Water is an integral part of protein complexes. It shapes protein binding sites by filling cavities and it bridges local contacts by hydrogen bonds. However, water molecules are usually not included in protein interface models in the past, and few

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