This enzyme is useful for enzymatic determination of NH₃, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease. This enzyme is also used for enzymatic determination of urea when coupled with urease in clinical analysis.
Tribioscience Glutamate dehydrogenase(NADP dependent), Enzyme Activity (TBP0023)
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Tribioscience Glutamate dehydrogenase(NADP dependent), Enzyme Activity (TBP0023)
Research Use Only. Not intended for human use.
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Preparation and Specification
Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN₃ and 5.0mM EDTA, pH 7.8
Activity: GradeⅡ∙Ⅲ 300U/mg-protein or more (9,000U/ml or more)
Contaminants: NADPH oxidase ≤1.0×10⁻²%
Glutathione reductase ≤1.0×10⁻²% (GradeⅡ-209) ≤1.0×10⁻¹% (GradeⅢ-309)
Stabilizer: Ethylenediaminetetraacetic acid (EDTA)
Properties
Stability: Stable at -20°C for at least One year
Molecular weight: approx. 300,000
Isoelectric point: 4.6
Michaelis constants: 1.1×10⁻³M (NH₃), 3.4×10⁻⁴M (α-Ketoglutarate)
1.2×10⁻³M (L-Glutamate), 1.4×10⁻⁵M (NADPH), 1.5×10⁻⁵M (NADP⁺)
Structure: 6 subunits (M.W.50,000) per enzyme molecule
Inhibitors: Hg⁺⁺, Cd⁺⁺, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine, 2,2′-dithiopyridine
Optimum pH: 8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG)
Optimum temperature: 45°C (α-KG→L-Glu) 45-55°C (L-Glu→α-KG)
pH Stability: pH 6.0-8.5 (25°C, 20hr)
Thermal stability: below 50°C (pH 7.4, 10min)
Applications