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 (URH-201) in clinical analysis.

 

Additional information

SIZE	1000 U, 5000 U

Datasheet:

TBP0024-Glutamate dehydrogenase(NAD dependent)

MSDS:

TBP0024_Glutamate dehydrogenase(NAD dependent) Safety Data Sheet