Glutamate dehydrogenase is an enzyme in both prokaryotes and eukaryotic mitochondria. Glutamate dehydrogenase can be used for the enzymatic determination of ammonia, alpha-ketoglutaric acid, L-glutamate and urease^[1].

Product Information
This product is recombinantly produced and can be used for the enzymatic determination of ammonia, α-ketoglutarate and L-glutamate, as well as the determination of leucine aminopeptidase and urease. In clinical analysis, this enzyme is combined with urease and can also be used for the enzymatic determination of urea.

Isoelectric point: 5.6
Michaelis constant: 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＋)
Optimum pH: 7.0-9.0
Optimum temperature: 50-55°C
pH stability: 5.0－10.0 (25°C, 20hr)
Thermal stability: below 50°C (pH 8.3, 10min)
Inhibitors: heavy metals, PCMB, IAA

Instructions
Soluble in 10 mM phosphate buffer (pH 7.0)

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

• [1]. S A Robinson, et al. The role of glutamate dehydrogenase in plant nitrogen metabolism. Plant Physiol. 1991 Feb;95(2):509-16.  [Content Brief]