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G2626

Sigma-Aldrich

L-Glutamic Dehydrogenase from bovine liver

Type II, 50% glycerol solution, ≥35 units/mg protein

Sinónimos:

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

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20 MG
$100.00
50 MG
$177.00
100 MG
$266.00
500 MG
$949.00

$100.00

Fecha estimada de envío14 de abril de 2025

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20 MG
$100.00
50 MG
$177.00
100 MG
$266.00
500 MG
$949.00

About This Item

Número de CAS:
9029-12-3
Comisión internacional de enzimas:
1.4.1.3 (BRENDA, IUBMB)
MDL number:
MFCD00131461
UNSPSC Code:
12352204
NACRES:
NA.54

$100.00

Fecha estimada de envío14 de abril de 2025

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biological source

bovine liver

Quality Level

200

type

Type II

form

glycerol solution (50%)

specific activity

≥35 units/mg protein

mol wt

310-350 kDa

UniProt accession no.

P00366

shipped in

wet ice

storage temp.

2-8°C

Gene Information

cow ... GLUD1(281785)

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Application

L-glutamic dehydrogenase was used to catalyze the conversion of isocitrate into α-ketoglutarate and carbon dioxide.[1]

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

50% glycerol solution

Analysis Note

Protein determined by biuret.

substrate

Referencia del producto
Descripción
Precios

K2010

α-Ketoglutaric acid sodium salt, BioUltra

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
0000385876
0000385876
0000401517
0000396268
0000373147

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Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.
Bezsudnova, et al.
PLoS ONE, 16, e0255098-e0255098 (2021)
S Vesce et al.
FEBS letters, 411(1), 107-109 (1997-07-07)
The mechanisms of HIV-1 neurotoxicity remain still undefined although the induction of signalling events and a modest inhibition of glutamate uptake induced by the envelope glycoprotein, gp120, have called attention to astrocytes. Here we demonstrate that the levels at which
Mariagrazia Grimaldi et al.
Human molecular genetics, 26(18), 3453-3465 (2017-09-16)
Congenital hyperinsulinism/hyperammonemia (HI/HA) syndrome gives rise to unregulated protein-induced insulin secretion from pancreatic beta-cells, fasting hypoglycemia and elevated plasma ammonia levels. Mutations associated with HI/HA were identified in the Glud1 gene, encoding for glutamate dehydrogenase (GDH). We aimed at identifying
Anna K Junk et al.
Molecular vision, 16, 1286-1291 (2010-07-29)
To determine whether activity of carbohydrate metabolism enzymes (aldolase, pyruvate kinase, isocitrate dehydrogenase, and malate dehydrogenase) are altered in the glaucomatous trabecular meshwork (TM) compared to controls. Tissue specimens were obtained from trabeculectomy (n=45 open angle glaucoma; Caucasian, average age
Mehran Karimi et al.
Seminars in thrombosis and hemostasis, 35(4), 426-438 (2009-07-15)
Factor XIII (FXIII) is a tetrameric zymogen (FXIII-A (2)B (2)) that is converted into an active transglutaminase (FXIIIa) by thrombin and Ca (2+) in the terminal phase of the clotting cascade. By cross-linking fibrin chains and alpha (2) plasmin inhibitor
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