G7509
GABase from Pseudomonas fluorescens
lyophilized powder, Protein ≥30 % by biuret
Synonyme(s) :
GABase Enzyme, GABase from Pseudomonas, Pseudomonas GABase
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About This Item
Produits recommandés
Source biologique
Pseudomonas fluorescens
Niveau de qualité
Essai
≥30 % (biuret)
Forme
lyophilized powder
Activité spécifique
≥0.5 units/mg protein
Composition
Protein, ≥30% biuret
Technique(s)
inhibition assay: suitable
Température de stockage
−20°C
Description générale
Research area: Neuroscience
GABase is a commercially available mixture composed of γ-aminobutyric acid aminotransferase (GABGT) and succinic semialdehyde dehydrogenase (SSDH) obtained from Pseudomonas fluorescens.
GABase is a commercially available mixture composed of γ-aminobutyric acid aminotransferase (GABGT) and succinic semialdehyde dehydrogenase (SSDH) obtained from Pseudomonas fluorescens.
Application
GABase from Pseudomonas fluorescens has been used for GABase assay to quantify the extracellular and intracellular concentration of GABA (γ-aminobutyric acid).
Actions biochimiques/physiologiques
GABase catalyzes the conversion of γ-aminobutyric acid (GABA) to succinic acid in the central nervous system. It is used to measure GABA levels in various biological samples. p-Hydroxybenzaldehyde (HBA) is known to be a potential inhibitor on GABase.
Définition de l'unité
One unit will convert 1.0 μmole of γ-aminobutyric acid (GABA) to succinic semialdehyde and then to succinate per min with a stoichiometric reduction of 1.0 μmole of NADP+ at pH 8.6 at 25 °C.
Forme physique
Partially purified lyophilized powder containing buffer salts and stabilizer
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Applied and environmental microbiology, 76(11), 3529-3537 (2010-04-20)
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The Biochemical journal, 229(3), 675-678 (1985-08-01)
L-threo-3-Fluoroglutamate and L-erythro-3-fluoroglutamate were tested with glutamate decarboxylase from Escherichia coli. Both isomers were substrates: the threo isomer was decarboxylated into optically active 4-amino-3-fluorobutyrate, whereas the erythro isomer lost the fluorine atom during the reaction, yielding succinic semialdehyde after hydrolysis
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Many studies have focussed on modulating the activity of γ-aminobutyric acid transaminase (GABA-T), a GABA-catabolizing enzyme, for treating neurological diseases, such as epilepsy and drug addiction. Nevertheless, human GABA-T synthesis and purification have not been established. Thus, biochemical and drug
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