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MilliporeSigma

10197734001

Roche

Glutamate Dehydrogenase (GlDH)

from beef liver

Synonym(s):

DNA marker

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About This Item

EC Number:
UNSPSC Code:
12352204
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biological source

bovine liver

Quality Level

form

lyophilized

specific activity

10 U/mg
~10 units/mg protein (at 25 °C with 2-oxoglutarate as the substrate, and ADP as the activator.)

packaging

pkg of 3,000 U

manufacturer/tradename

Roche

concentration

≥10-20 % (w/w)

technique(s)

activity assay: suitable

color

white

optimum pH

8

solubility

water: 20 mg/mL, colorless

suitability

suitable for UV spectrophotometry and general use

UniProt accession no.

application(s)

life science and biopharma

foreign activity

ADH <0.00500%
LDH <0.00500%
MDH <0.00500%

shipped in

wet ice

storage temp.

2-8°C

Gene Information

bovine ... GLUD1(281785)

General description

Approximately 10 U/mg lyophilizate (120 U/mg enzyme protein) at +25°C with 2-oxoglutarate as the substrate, and ADP as the activator.
GDH (Glutamate dehydrogenase) is a hexamer of 449 residues and is located in the mitochondria. It acts as a branch-point enzyme between amino acid oxidation and urea production. L-glutamate:NAD(P)+ oxidoreductase is involved in deamination.

Application

Glutamate dehydrogenase has been used to measure residual ammonium by enzymatic analysis during fermentation by wine yeast. It used as a component of cofactor recycling systems for NAD(P) and NAD(P)H.

Analysis Note

Contaminants: <0.005% ADH, LDH, and MDH, each

Other Notes

For life science research only. Not for use in diagnostic procedures.
The smallest active structure of GIDH (310,000 to 350,000 ) is a hexamer subunit of 55,400 D. This hexamer reversibly self-assembles forming a polymer with up to eight hexamers (2,200 kD).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash


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Disruption of the cell wall integrity gene ECM33 results in improved fermentation by wine yeast
Jin Zhang
Metabolic engineering (2018)
T J Stillman et al.
Journal of molecular biology, 234(4), 1131-1139 (1993-12-20)
We have solved the structure of the binary complex of the glutamate dehydrogenase from Clostridium symbiosum with glutamate to 1.9 A resolution. In this complex, the glutamate side-chain lies in a pocket on the enzyme surface and a key determinant
P J O'Brien et al.
Laboratory animals, 36(3), 313-321 (2002-07-30)
In a recent study in rats, alanine aminotransferase (ALT), the preferred plasma biomarker of hepatocellular injury in rats, was ineffective at detecting marked hepatic necrosis produced by acetaminophen (Human and Experimental Toxicology 19, 277-83, 2000). In contrast, glutamate dehydrogenase (GLDH)

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