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G2626

Sigma-Aldrich

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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2 MG
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2 MG
908,00 $

About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

908,00 $


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biological source

bovine liver

Quality Level

type

Type II

form

glycerol solution (50%)

specific activity

≥35 units/mg protein

mol wt

310-350 kDa

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

Gene Information

cow ... GLUD1(281785)

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This Item
D9250D9500D4010
Quality Level

100

Quality Level

200

Quality Level

200

Quality Level

200

assay

≥90% (HPLC)

assay

≥90% (HPLC)

assay

≥99% (HPLC)

assay

≥96% (HPLC)

form

powder

form

powder

form

powder

form

powder

solubility

water: 5 mg/mL, clear, colorless

solubility

water: 50 mg/mL, clear, colorless

solubility

water: 50 mg/mL, clear, colorless

solubility

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Gene Information

human ... HRAS(3265)

Gene Information

-

Gene Information

-

Gene Information

-

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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H Zhang et al.
Antiviral research, 24(1), 43-57 (1994-05-01)
Two mutants of HIV-1 reverse transcriptase (RT), Tyr-188-->His and Glu-138-->Arg have been prepared and their catalytic properties and sensitivities to inhibitors studied. As compared to wild type RT, a reduction in catalytic efficiency and turn over number was observed, especially
Z Debyser et al.
The Journal of biological chemistry, 267(17), 11769-11776 (1992-06-15)
Recently, tetrahydroimidazo-[4,5,1-jk][1,4]-benzodiazepin-2(1H)-one and -thione (TIBO) and 1-[(2-hydroxyethoxy)methyl]-6-(phenylthio)thymine (HEPT) compounds have been shown to be potent, selective, and specific inhibitors of human immunodeficiency virus type 1 (HIV-1) replication in vitro. They interact with the reverse transcriptase of HIV-1 in a way
Nathan A Tanner et al.
Nucleic acids research, 37(4), e27-e27 (2009-01-22)
We present a simple technique for visualizing replication of individual DNA molecules in real time. By attaching a rolling-circle substrate to a TIRF microscope-mounted flow chamber, we are able to monitor the progression of single-DNA synthesis events and accurately measure
Tadamasa Sasaki et al.
The Plant journal : for cell and molecular biology, 47(5), 802-810 (2006-07-22)
RNA editing is found in various transcripts from land plant chloroplasts. In tobacco chloroplasts, C-to-U conversion occurs at 36 specific sites including two sites identified in this work. Our RNA editing assay system using chloroplast extracts facilitated biochemical analyses of
H Jonckheere et al.
The Journal of biological chemistry, 269(41), 25255-25258 (1994-10-14)
Determination of the three-dimensional structure of the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) has indicated a totally different folding for the 51-kDa subunit (p51) than for the 66-kDa subunit (p66). The polymerase catalytic site is located on the

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