G6637
β-Galactose Dehydrogenase from Pseudomonas fluorescens
recombinant, expressed in E. coli, ammonium sulfate suspension, ≥50 units/mg protein (biuret)
Synonym(s):
D-Galactose:NAD+ 1-oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-837-4
MDL number:
Specific activity:
≥50 units/mg protein (biuret)
Assay:
0.5—2.0 mg protein/mL (biuret)
Biological source:
Pseudomonas fluorescens
Recombinant:
expressed in E. coli
biological source
Pseudomonas fluorescens
recombinant
expressed in E. coli
assay
0.5—2.0 mg protein/mL (biuret)
form
ammonium sulfate suspension
specific activity
≥50 units/mg protein (biuret)
color
white
suitability
suitable for enzyme test
application(s)
life science and biopharma
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Gene Information
Pseudomonas fluorescens ... gdh(533113295)
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Application
β-Galactose Dehydrogenase from Pseudomonas fluorescens has been used for competitive inhibition in lectin histochemistry. It has also been used to measure the hydrolysis activity of Haloferax alicantei β-galactosidase on different disaccharides.
Biochem/physiol Actions
β-galactose dehydrogenase catalyzes the oxidation of β-D-galactose to D-galactono-gammalactone.
Physical form
Suspension in 3.2 M (NH4)2SO4, pH approx. 6.0
Other Notes
One unit will convert 1.0 μmole of D-galactose to D-galactonate per min at pH 8.6 at 25 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Takahiro Mieda et al.
Plant & cell physiology, 45(9), 1271-1279 (2004-10-29)
We have studied the enzymological properties of L-galactose dehydrogenase (l-GalDH), a key enzyme in the biosynthetic pathway of l-ascorbate (AsA) in plants. L-GalDH was purified approximately 560-fold from spinach leaves. The enzyme was a homodimer with a subunit mass of
Optimizing the enzymatic determination of galactose in the culture medium of rat liver and HepG2 cell spheroids.
Jinsheng Xu et al.
Analytical biochemistry, 311(2), 179-181 (2002-12-10)
D Peltzer et al.
Free radical research, 31 Suppl, S181-S185 (2000-02-29)
Green and white variegated leaves of Coleus blumei, Benth. were separated into albino and green sections and used to determine the distribution of vitamin C and L-galactose dehydrogenase activity, an enzyme supposed to be involved in ascorbate metabolism, in heterotrophic
C F Mazitsos et al.
European journal of biochemistry, 269(22), 5391-5405 (2002-11-09)
Protein molecular modelling and ligand docking were employed for the design of anthraquinone galactosyl-biomimetic dye ligands (galactosyl-mimodyes) for the target enzyme galactose dehydrogenase (GaDH). Using appropriate modelling methodology, a GaDH model was build based on a glucose-fructose oxidoreductase (GFO) protein
Stephan Gatzek et al.
The Plant journal : for cell and molecular biology, 30(5), 541-553 (2002-06-06)
l-Galactose dehydrogenase (l-GalDH), a novel enzyme that oxidizes l-Gal to l-galactono-1,4-lactone (l-GalL), has been purified from pea seedlings and cloned from Arabidopsis thaliana. l-GalL is a proposed substrate for ascorbate biosynthesis in plants, therefore the function of l-GalDH in ascorbate
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