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G7882

L-Glutamic Dehydrogenase from bovine liver

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

Synonym(s):

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

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100 MG

4 110,00 kr

500 MG

19 370,00 kr

1 G

29 190,00 kr

4 110,00 kr

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About This Item

CAS Number:
9029-12-3
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-848-4
MDL number:
MFCD00131461
EC Number:
1.4.1.3 (BRENDA, IUBMB)

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Product Name

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

biological source

bovine liver

type

Type III

form

lyophilized powder

specific activity

≥20 units/mg protein

UniProt accession no.

P00366

storage temp.

−20°C

Quality Level

200

Gene Information

cow ... GLUD1(281785)

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G2501G2626L1378
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-Glutamic Dehydrogenase from bovine liver Type II, 50% glycerol solution, ≥35 units/mg protein

Sigma-Aldrich

G2626

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

biological source

bovine liver

biological source

-

biological source

bovine liver

biological source

bovine muscle

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

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

specific activity

≥20 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥35 units/mg protein

specific activity

≥600 units/mg protein

form

lyophilized powder

form

ammonium sulfate suspension

form

glycerol solution (50%)

form

ammonium sulfate suspension

UniProt accession no.

P00366

UniProt accession no.

P00366

UniProt accession no.

P00366

UniProt accession no.

P19858, Q5E9B1

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Analysis Note

Protein determined by biuret

Application

L-Glutamic Dehydrogenase was used to catalyzes the conversion of isocitrate into a-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.

Packaging

Package size based on protein content

Physical form

Contains citrate and potassium phoshate buffer salts.

used together

Product No.
Description
Pricing

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000484428
0000484440
0000484428
0000484440
0000449205

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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
Aidan P France et al.
Analytical chemistry, 92(6), 4340-4348 (2020-02-14)
Careful transfer of ions into the gas-phase permits the measurement of protein structures, with ion mobility-mass spectrometry, which provides shape and stoichiometry information. Collision cross sections (CCS) can be obtained from measurements made of the ions mobility through a given
View All Related Papers

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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

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