C1261
Carboxypeptidase A−Agarose
ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, enzyme from bovine pancreas
别名:
Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
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关于此项目
Specific activity:
≥6 units/mL packed gel, 25 °C
Biological source:
enzyme from bovine pancreas
biological source
enzyme from bovine pancreas
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
Quality Level
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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
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
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
3. Carboxypeptidase. Bovine carboxypeptidase A--activation, chemical structure and molecular heterogeneity.
H Neurath et al.
Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 257(813), 159-176 (1970-02-12)
实验方案
Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.
在测定羧肽酶A活性时，使用马尿酸-L-苯丙氨酸在254nm处进行连续分光光度法测定。羧肽酶A水解C末端残基上的肽键。
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