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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
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$360.00
500 mg
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$1,420.00
1 g
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$2,130.00

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)
Specific activity:
≥20 units/mg protein
Biological source:
bovine liver

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biological source

bovine liver

Quality Segment

200

type

Type III

form

lyophilized powder

specific activity

≥20 units/mg protein

UniProt accession no.

P00366

storage temp.

−20°C

Gene Information

cow ... GLUD1(281785)

Application

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

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.

Packaging

Package size based on protein content

Physical form

Contains citrate and potassium phoshate buffer salts.

Analysis Note

Protein determined by biuret

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.

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

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L1378

L-Lactic Dehydrogenase from bovine muscle

description

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

description

Type I, ammonium sulfate suspension, ≥40 units/mg protein

description

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

description

Type X, ammonium sulfate suspension, ≥600 units/mg protein

specific activity

≥20 units/mg protein

specific activity

≥40 units/mg protein

specific activity

≥35 units/mg protein

specific activity

≥600 units/mg protein

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)

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.

Q5E9B1, P19858

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

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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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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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