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G2626

L-Glutamic Dehydrogenase from bovine liver

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

Synonym(s):

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

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20 MG

985,00 kr

50 MG

1 940,00 kr

100 MG

3 380,00 kr

500 MG

13 160,00 kr

985,00 kr

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About This Item

CAS Number:
9029-12-3
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
1.4.1.3 (BRENDA, IUBMB)
MDL number:
MFCD00131461

Key Documents

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Product Name

L-Glutamic Dehydrogenase from bovine liver, Type II, 50% glycerol solution, ≥35 units/mg protein

biological source

bovine liver

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

Quality Level

200

Gene Information

cow ... GLUD1(281785)

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G7882G2501L1378
L-Glutamic Dehydrogenase from bovine liver Type II, 50% glycerol solution, ≥35 units/mg protein

Sigma-Aldrich

G2626

L-Glutamic Dehydrogenase from bovine liver

L-Glutamic Dehydrogenase from bovine liver Type III, lyophilized powder, ≥20 units/mg protein

Sigma-Aldrich

G7882

L-Glutamic Dehydrogenase from bovine liver

L-Glutamic Dehydrogenase from bovine liver Type I, ammonium sulfate suspension, ≥40 units/mg protein

Sigma-Aldrich

G2501

L-Glutamic Dehydrogenase from bovine liver

L-Lactic Dehydrogenase from bovine muscle Type X, ammonium sulfate suspension, ≥600 units/mg protein

Sigma-Aldrich

L1378

L-Lactic Dehydrogenase from bovine muscle

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... LDHA(281274), LDHB(281275)

biological source

bovine liver

biological source

bovine liver

biological source

-

biological source

bovine muscle

specific activity

≥35 units/mg protein

specific activity

≥20 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥600 units/mg protein

form

glycerol solution (50%)

form

lyophilized powder

form

ammonium sulfate suspension

form

ammonium sulfate suspension

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

UniProt accession no.

P00366

UniProt accession no.

P00366

UniProt accession no.

P00366

UniProt accession no.

P19858, Q5E9B1

Analysis Note

Protein determined by biuret.

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.

Other Notes

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

used together

Product No.
Description
Pricing

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000450225
0000450225
0000497752
0000497752
0000474910

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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
Vedrana Montana et al.
Neurochemical research, 46(10), 2551-2579 (2021-06-01)
Astrocytes have a prominent role in metabolic homeostasis of the brain and can signal to adjacent neurons by releasing glutamate via a process of regulated exocytosis. Astrocytes synthesize glutamate de novo owing to the pyruvate entry to the citric/tricarboxylic acid
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)
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
Virginia Kroef et al.
eLife, 11 (2022-03-02)
The hexosamine biosynthetic pathway (HBP) produces the essential metabolite UDP-GlcNAc and plays a key role in metabolism, health, and aging. The HBP is controlled by its rate-limiting enzyme glutamine fructose-6-phosphate amidotransferase (GFPT/GFAT) that is directly inhibited by UDP-GlcNAc in a
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HPLC Analysis of Protein Standards (1) on BIOshell™ A400 Protein C4

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