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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥35 units/mg protein
Biological source:
bovine liver
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Laissez-nous vous aiderbiological source
bovine liver
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
Quality Level
Gene Information
cow ... GLUD1(281785)
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Application
L-glutamic dehydrogenase was used to catalyze the conversion of isocitrate into α-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:
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
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.
Physical form
50% glycerol solution
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.
Classe de stockage
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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