Glutamate dehydrogenase(NAD dependent), Enzyme Activity (TBP0024)

Description

Preparation and Specification

Appearance: White amorphous powder, lyophilized

Activity: GradeⅡ 100 U/mg-solid or more

Contaminants: NAD oxidase ≤1.0×10⁻²%

Properties

Stability: Stable at -20°C for at least One year

Molecular weight: approx. 260,000

Isoelectric point: 5.6

Michaelis constants: 9.21×10⁻³M (NH₃), 4.80×10⁻³M (α-Ketoglutarate)

7.8×10⁻⁵M (L-Glutamate), 1.29×10⁻⁴M (NADH), 5.89×10⁻⁴M (NAD⁺)

Structure: 6 subunits per enzyme molecule

Inhibitors: Heavy metals, PCMB, IAA

Optimum pH: 7.5-8.0 (α-KG→L-Glu) 9.0 (L-Glu→α-KG)

Optimum temperature: 55°C (α-KG→L-Glu) 50°C (L-Glu→α-KG)

pH Stability: pH 5.0-10.0 (25°C, 20hr)

Thermal stability: below 50°C (pH 8.3, 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:

TBP0024-Glutamate dehydrogenase(NAD dependent)

MSDS:

TBP0024_Glutamate dehydrogenase(NAD dependent) Safety Data Sheet

Research use only.