Glutamate dehydrogenase(NADP dependent), Enzyme Activity (TBP0023)

Description

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

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.

Research use only.

Additional information

Datasheet:

TBP0023-Glutamate dehydrogenase(NADP dependent)

MSDS:

TBP0023_Glutamate dehydrogenase(NADP dependent) Safety Data Sheet

Research use only.