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Merck
CN

A5384

Aconitase from porcine heart

别名:

Aconitate hydratase, Citrate (isocitrate) hydrolyase

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Biological source:
Porcine heart
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biological source

Porcine heart

form

solid

mol wt

~66 kDa by gel filtration

storage temp.

−20°C

Quality Level

Analysis Note

Crude preparation containing aconitase activity

Application

Aconitase may be usefull in diabetes research as well as to study structural conservation between iron-responsive element binding proteins (IRE-BP) and isomerases .

Biochem/physiol Actions

Aconitase catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle. Aconitase is inhibited by cyanide, sulfide and copper and mercury at low concentrations. It is competitively inhibited by trans-aconitate. Aconitase contains an internal Fe-S cluster which is responsible for its activity.

Other Notes

One unit will convert 1.0 μmole of citrate (via cis-aconitate) to isocitrate per min at pH 7.4 at 25 °C.

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

动植物源性产品
低风险生物材料
此项目有

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分析证书(COA)

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Ewelina Michta et al.
Environmental microbiology, 14(12), 3203-3219 (2012-11-03)
In many organisms, aconitases have dual functions; they serve as enzymes in the tricarboxylic acid cycle and as regulators of iron metabolism. In this study we defined the role of the aconitase AcnA in Streptomyces viridochromogenes Tü494, the producer of
Lucy M Hinder et al.
The Journal of endocrinology, 216(1), 1-11 (2012-10-23)
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S S Popov et al.
Eksperimental'naia i klinicheskaia farmakologiia, 75(7), 32-35 (2012-10-03)
A combined therapy with melaxen led to a decrease in the activity of gamma-glutamyl transpeptidase and the level of diene conjugates in blood serum of patients with the drug-induced hepatitis developing on the background of administration of antituberculous preparations. These
Béatrice Py et al.
Molecular microbiology, 86(1), 155-171 (2012-09-13)
Biosynthesis of iron-sulphur (Fe-S) proteins is catalysed by multi-protein systems, ISC and SUF. However, 'non-ISC, non-SUF' Fe-S biosynthesis factors have been described, both in prokaryotes and eukaryotes. Here we report in vitro and in vivo investigations of such a 'non-ISC

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