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G7882

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

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

Sinonimo/i:

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

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100 MG
CHF 477.00
500 MG
CHF 1’780.00
1 G
CHF 2’970.00

CHF 477.00

Spedizione prevista il29 maggio 2025

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Cambia visualizzazione
100 MG
CHF 477.00
500 MG
CHF 1’780.00
1 G
CHF 2’970.00

About This Item

Numero CAS:
9029-12-3
Classificazione EC (Enzyme Commission):
1.4.1.3 (BRENDA, IUBMB)
Numero CE:
232-848-4
Numero MDL:
MFCD00131461
Codice UNSPSC:
12352204
NACRES:
NA.54

CHF 477.00

Spedizione prevista il29 maggio 2025

Origine biologica

bovine liver

Livello qualitativo

200

Tipo

Type III

Stato

lyophilized powder

Attività specifica

≥20 units/mg protein

N° accesso UniProt

P00366

Temperatura di conservazione

−20°C

Informazioni sul gene

cow ... GLUD1(281785)

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Applicazioni

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

Azioni biochim/fisiol

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.

Confezionamento

Package size based on protein content

Definizione di unità

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.

Stato fisico

Contains citrate and potassium phoshate buffer salts.

Risultati analitici

Protein determined by biuret

Substrato

N° Catalogo
Descrizione
Determinazione del prezzo

Pittogrammi

Health hazard
GHS08

Avvertenze

Danger

Indicazioni di pericolo

H334

Consigli di prudenza

P261 - P284 - P501

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

Lot/Batch Number
0000284146
0000284155
SLCR0568
SLCK9206
SLCH8002

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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
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
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)
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
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
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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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