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G7882

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

Type III, lyophilized powder, ≥20 units/mg protein

Sinónimos:

L-GLDH, L-Glutamate:NAD[P]+ Oxidoreductase (deaminating), Glutamate Dehydrogenase from bovine liver

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100 MG
$255.000
500 MG
$1.010.000
1 G
$1.520.000

$255.000

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100 MG
$255.000
500 MG
$1.010.000
1 G
$1.520.000

About This Item

Número de CAS:
9029-12-3
Comisión internacional de enzimas:
1.4.1.3 (BRENDA, IUBMB)
Número CE:
232-848-4
Número MDL:
MFCD00131461
Código UNSPSC:
12352204
NACRES:
NA.54

$255.000

En stockDetalles

origen biológico

bovine liver

Nivel de calidad

200

tpo

Type III

Formulario

lyophilized powder

actividad específica

≥20 units/mg protein

Nº de acceso UniProt

P00366

temp. de almacenamiento

−20°C

Información sobre el gen

cow ... GLUD1(281785)

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Aplicación

L-Glutamic Dehydrogenase was used to catalyzes the conversion of isocitrate into a-ketoglutarate and carbon dioxide.[1]

Acciones bioquímicas o fisiológicas

Mammalian forms of this enzyme, including this bovine form, can use either NADP(H) or NAD(H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species.

The bovine enzyme is characterized by three sets of properties:
  • It has a reversible concentration-dependent association, producing higher molecular weight forms.
  • Forms tight enzyme-reduced coenzyme-substrate ternary complexes whose rates of dissociation modulate the steady-state reaction rates.
  • Exhibits a wide variety of effects from the binding of any of a number of nucleotide modifiers.

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

Envase

Package size based on protein content

Definición de unidad

One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.3 at 25 °C, in the presence of ammonium ions.

Forma física

Contains citrate and potassium phoshate buffer salts.

Nota de análisis

Protein determined by biuret

sustrato

Referencia del producto
Descripción
Precios

K2010

α-Ketoglutaric acid sodium salt, BioUltra

Pictogramas

Health hazard
GHS08

Palabra de señalización

Danger

Frases de peligro

H334

Consejos de prudencia

P261 - P284 - P501

Clasificaciones de peligro

Resp. Sens. 1

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
0000284146
0000284146
0000284155
0000284155
SLCR0568

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Laszlo Tretter et al.
Journal of neurochemistry, 83(4), 855-862 (2002-11-08)
Previously we have reported that oxidative stress induced by hydrogen peroxide exacerbates the effect of an Na+ load in isolated nerve terminals, with a consequence of an ATP depletion, [Ca2+]i and [Na+]i deregulation, and collapse of mitochondrial membrane potential. In
Roy M Daniel et al.
The Biochemical journal, 425(2), 353-360 (2009-10-24)
Experimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model based on increases in activity and denaturation. The Equilibrium Model provides a quantitative explanation of enzyme thermal behaviour under reaction
Decreased carbohydrate metabolism enzyme activities in the glaucomatous trabecular meshwork
Junk AK, Goel M, Mundorf T, Rockwood EJ, Bhattacharya SK
Molecular Vision, 10, 1286-1291 (2010)
Vasily A Aleshin et al.
International journal of molecular sciences, 23(19) (2022-10-15)
Glutamate dehydrogenase (GDH) plays a key role in the metabolism of glutamate, an important compound at a cross-road of carbon and nitrogen metabolism and a relevant neurotransmitter. Despite being one of the first discovered allosteric enzymes, GDH still poses challenges
S M Kuo et al.
Biology of the neonate, 43(1-2), 23-32 (1983-01-01)
The tissue distribution, the subcellular distribution in liver, and the developmental patterns of cysteine:alpha-ketoglutarate aminotransferase (CAT) and 3-mercaptopyruvate sulfurtransferase (MPST) activities were determined in rats of the Sprague-Dawley strain. CAT activity was highest in heart and liver, whereas MPST activity
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Questions

  1. L-グルタミン酸デヒドロゲナーゼ ウシ肝臓由来（製品番号G7882）のKm値（Properties）や至適pH（Specificity）の情報を提供いただけませんでしょうか。

    1 answer

    1. The Km values for this product have not been determined. Please see the link below to review a reference that may be helpful:
      https://www.jbc.org/article/S0021-9258(19)83816-4/pdf

      The activity of this enzyme is determined at pH 7.3 at 25 °C. Please see the link below to review the product assay protocol:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/137/309/g7882enz.pdf

      Helpful?

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