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
产品名称
Carboxypeptidase A−Agarose, ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, 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
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.
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.
Other Notes
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
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
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
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
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
Hilana Salete Silva Oliveira et al.
Journal of food science, 76(5), C755-C759 (2012-03-16)
This paper proposes a method to enzymatically treat poor-quality cocoa almonds (known as "slate") to ensure the formation of chocolate flavor precursors. The production of flavor precursors improves the quality of these almonds, which are usually responsible for the low
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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