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Merck
CN

C1261

Sigma-Aldrich

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

MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54
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生物来源

enzyme from bovine pancreas

表单

ammonium sulfate suspension

比活

≥6 units/mL packed gel, 25 °C

分子量

~35,250

基质

beaded agarose

储存温度

2-8°C

一般描述

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

生化/生理作用

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.

外形

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

其他说明

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

象形图

Health hazardExclamation mark

警示用语:

Danger

危险分类

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

靶器官

Respiratory system

储存分类代码

10 - Combustible liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

新产品
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
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
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
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

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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