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C1261

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

EC Number:
3.4.17.1 (BRENDA, IUBMB)
MDL number:
MFCD00130718
UNSPSC Code:
12352204
NACRES:
NA.54

Key Documents

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biological source

enzyme from bovine pancreas

Quality Level

200

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

Related Categories

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.

Physical form

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

Other Notes

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

pictograms

Health hazardExclamation mark
GHS08,GHS07

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

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Certificates of Analysis (COA)

Lot/Batch Number
0000257065
0000269905
SLBR9434V
050K7020
050K70201

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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
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
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
Sandeep Chakraborty et al.
PloS one, 7(2), e32011-e32011 (2012-02-24)
Promiscuity, the basis for the evolution of new functions through 'tinkering' of residues in the vicinity of the catalytic site, is yet to be quantitatively defined. We present a computational method Promiscuity Indices Estimator (PROMISE)--based on signatures derived from the
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Protocols

Enzymatic Assay: Carboxypeptidase

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

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