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About This Item
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
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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
Sahar I Da'as et al.
Blood, 119(15), 3585-3594 (2012-03-01)
We used the opportunities afforded by the zebrafish to determine upstream pathways regulating mast cell development in vivo and identify their cellular origin. Colocalization studies demonstrated zebrafish notch receptor expression in cells expressing carboxypeptidase A5 (cpa5), a zebrafish mast cell-specific
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
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
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.
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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