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Merck

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:
9028-54-0
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-837-4
MDL number:
MFCD00130622
EC Number:
1.1.1.48 (BRENDA, IUBMB)
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

Key Documents

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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

200

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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Certificates of Analysis (COA)

Lot/Batch Number
SLCH3542
SLBZ8176
SLBX5742
SLBR7772V
SLBN1974V

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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
T E Curey et al.
Analytical biochemistry, 293(2), 178-184 (2001-06-12)
We report the development of a sensor for rapidly and simultaneously measuring multiple sugars in aqueous samples. In this strategy, enzyme-based assays are localized within an array of individually addressable sites on a micromachined silicon chip. Microspheres derivatized with monosaccharide-specific
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
Robert D Hancock et al.
BMC plant biology, 3, 7-7 (2003-11-25)
Although plants are the main source of vitamin C in the human diet, we still have a limited understanding of how plants synthesise L-ascorbic acid (AsA) and what regulates its concentration in different plant tissues. In particular, the enormous variability
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Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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