G7882
L-Glutamic Dehydrogenase from bovine liver
Type III, lyophilized powder, ≥20 units/mg protein
Sinónimos:
L-GLDH, L-Glutamate:NAD[P]+ Oxidoreductase (deaminating), Glutamate Dehydrogenase from bovine liver
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About This Item
Productos recomendados
origen biológico
bovine liver
Nivel de calidad
tpo
Type III
Formulario
lyophilized powder
actividad específica
≥20 units/mg protein
Nº de acceso UniProt
temp. de almacenamiento
−20°C
Información sobre el gen
cow ... GLUD1(281785)
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Aplicación
L-Glutamic Dehydrogenase was used to catalyzes the conversion of isocitrate into a-ketoglutarate and carbon dioxide.
Acciones bioquímicas o fisiológicas
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.
Envase
Package size based on protein content
Definición de unidad
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.
Forma física
Contains citrate and potassium phoshate buffer salts.
Nota de análisis
Protein determined by biuret
sustrato
Referencia del producto
Descripción
Precios
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Resp. Sens. 1
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Certificados de análisis (COA)
Lot/Batch Number
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Los clientes también vieron
Roy M Daniel et al.
The Biochemical journal, 425(2), 353-360 (2009-10-24)
Experimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model based on increases in activity and denaturation. The Equilibrium Model provides a quantitative explanation of enzyme thermal behaviour under reaction
Laszlo Tretter et al.
Journal of neurochemistry, 83(4), 855-862 (2002-11-08)
Previously we have reported that oxidative stress induced by hydrogen peroxide exacerbates the effect of an Na+ load in isolated nerve terminals, with a consequence of an ATP depletion, [Ca2+]i and [Na+]i deregulation, and collapse of mitochondrial membrane potential. In
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Junk AK, Goel M, Mundorf T, Rockwood EJ, Bhattacharya SK
Molecular Vision, 10, 1286-1291 (2010)
S M Kuo et al.
Biology of the neonate, 43(1-2), 23-32 (1983-01-01)
The tissue distribution, the subcellular distribution in liver, and the developmental patterns of cysteine:alpha-ketoglutarate aminotransferase (CAT) and 3-mercaptopyruvate sulfurtransferase (MPST) activities were determined in rats of the Sprague-Dawley strain. CAT activity was highest in heart and liver, whereas MPST activity
James K Kranz et al.
Methods in molecular biology (Clifton, N.J.), 796, 3-17 (2011-11-05)
Thermodynamic principles of cooperativity and allostery have long been used as a starting point to begin understanding the interplay between ligand binding events. Understanding the nature of allosteric effects requires an experimental technique that can be used to quantify ligand
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