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 (URH-201) in clinical analysis.

Additional information

SIZE	1000 U, 5000 U

Datasheet:

TBP0023-Glutamate dehydrogenase(NADP dependent)

MSDS:

TBP0023_Glutamate dehydrogenase(NADP dependent) Safety Data Sheet