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G2501

L-Glutamic Dehydrogenase from bovine liver

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

Synonym(s):

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

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20 MG

801,00 kr

50 MG

1 170,00 kr

100 MG

2 080,00 kr

801,00 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 I, ammonium sulfate suspension, ≥40 units/mg protein

type

Type I

form

ammonium sulfate suspension

specific activity

≥40 units/mg protein

mol wt

310-350 kDa

UniProt accession no.

P00366

storage temp.

2-8°C

Quality Level

200

Gene Information

cow ... GLUD1(281785)

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

Sigma-Aldrich

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Sigma-Aldrich

G7882

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

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

cow ... GLUD1(281785)

Gene Information

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

specific activity

≥40 units/mg protein

specific activity

≥20 units/mg protein

specific activity

≥35 units/mg protein

specific activity

≥600 units/mg protein

form

ammonium sulfate suspension

form

lyophilized powder

form

glycerol solution (50%)

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

mol wt

310-350 kDa

mol wt

-

mol wt

310-350 kDa

mol wt

-

Analysis Note

Protein determined by biuret

Biochem/physiol Actions

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.[1][2]
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

Suspension in 2.0 M (NH4)2SO4 solution

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
0000486814
0000486814
BCBB4624
SLCL5583
SLCD9985

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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
Hyperinsulinism and hyperammonaemia syndrome and severe myoclonic epilepsy of infancy.
F Pérez Errazquin et al.
Neurologia (Barcelona, Spain), 26(4), 248-252 (2010-12-18)
Glutamic dehydrogenase.
H J STRECKER
Archives of biochemistry and biophysics, 46(1), 128-140 (1953-09-01)
Cleanthe Spanaki et al.
Neurotoxicity research, 21(1), 117-127 (2011-11-01)
Glutamate dehydrogenase (GDH) catalyzes the reversible inter-conversion of glutamate to α-ketoglutarate and ammonia. High levels of GDH activity is found in mammalian liver, kidney, brain, and pancreas. In the liver, GDH reaction appears to be close-to-equilibrium, providing the appropriate ratio
Shanti Balasubramaniam et al.
Journal of pediatric endocrinology & metabolism : JPEM, 24(7-8), 573-577 (2011-09-22)
Hyperinsulinism-hyperammonemia syndrome (HI/HA) (OMIM 606762), the second most common form of congenital hyperinsulinism (CHI) is associated with activating missense mutations in the GLUD1 gene, which encodes the mitochondrial matrix enzyme, glutamate dehydrogenase (GDH). Patients present with recurrent symptomatic postprandial hypoglycemia
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