ʟ-Glutamic Dehydrogenase (NADP) from Proteus sp.,5000UNITS,G4387-5KU,Sigma

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订货号 0BP1313
品牌型号 Sigma G4387-5KU
货期 询货期
最小订货量 1件
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产品介绍 Product Description

General description

Isoelectric point : 4.6
Michaelis constants : 1.1 X 10-3M (NH3), 3.4 X 10-4M (α-Ketoglutarate)
1.2 X 10-3M (L-Glutamate), 1.4 X 10-5M (NADPH), 1.5 X 10-5M (NADP+)
Structure : 6 subunits (M.W.50,000) per mol of enzyme
Inhibitors : Hg++, Cd++, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine,
2,2′-dithiopyridine
Optimum pH : 8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG)
Optimum temperature : 45oC(α-KG−L-Glu) 45-55oC (L-Glu→α-KG)
pH stability : pH 6.0 - 8.5 (25oC, 20hr)
Thermal stability : below 50oC (pH 7.4, 10min)


Application

This enzyme is useful for enzymatic determination of NH3, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease. This enzyme is also used for enzymatic determination of urea when coupled with urease (URH-201) in clinical analysis. In vitro, various activity assays of this enzyme examine the conversion of α-ketoglutarate to L-glutamate, in the presence of excess ammonium ions (NH4+) and NADPH.


Biochem/physiol Actions

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.


Physical form

Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide


Other Notes

Note: Do not confuse with non-specific L-GLDH, EC 1.4.1.3.
One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30 °C in the presence of ammonium ions and NADPH.


技术参数 Specifications
biological sourcebacterial (Proteus spp.)
Quality Level200
formbuffered aqueous solution
specific activity≥4,000 units/mL
mol wt ~300 kDa
storage temp.2-8°C
长度(mm)
宽度(mm)
高度(mm)
重量(kg)
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