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L-Glutamic Dehydrogenase from bovine liver

SIGMA/G7882 - Type III, lyophilized powder, ≥20 units/mg protein

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

CAS Number: 9029-12-3
EC Number: 232-848-4
MDL Number: MFCD00131461
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-G7882-100MG 100 mg
$360.00
1/EA
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45-G7882-500MG 500 mg
$1420.00
1/EA
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45-G7882-1G 1 g
$2130.00
1/EA
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This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: G7882-1G
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: G7882-100MG
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: G7882-500MG

 

biological source bovine liver
form lyophilized powder
Quality Level 200 
specific activity ≥20 units/mg protein
storage temp. −20°C
type Type III
UniProt accession no. P00366 
Analysis Note: Protein determined by biuret
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.
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: 1 g in poly bottle
Packaging: 100, 500 mg in poly bottle
Packaging: Package size based on protein content
Physical form: Contains citrate and potassium phoshate buffer salts.
RIDADR NONH for all modes of transport
WGK Germany WGK 3
Flash Point(F) Not applicable
Flash Point(C) Not applicable
activity specific activity: ≥20 units/mg protein
Storage Temp. −20°C
Enzyme Commission (EC) Number 1.4.1.3   ( BRENDA  | IUBMB  )
UNSPSC 12352204

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