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Merck
CN

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)

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Product Name

β-Galactose Dehydrogenase from Pseudomonas fluorescens, recombinant, expressed in E. coli, ammonium sulfate suspension, ≥50 units/mg protein (biuret)

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.

Other Notes

One unit will convert 1.0 μmole of D-galactose to D-galactonate per min at pH 8.6 at 25 °C.

Physical form

Suspension in 3.2 M (NH4)2SO4, pH approx. 6.0

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
SLCH3542
SLBZ8176
SLBX5742
SLBR7772V
SLBN1974V

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Michael Sauer et al.
Applied and environmental microbiology, 70(10), 6086-6091 (2004-10-07)
Yeasts do not possess an endogenous biochemical pathway for the synthesis of vitamin C. However, incubated with l-galactose, L-galactono-1,4-lactone, or L-gulono-1,4-lactone intermediates from the plant or animal pathway leading to l-ascorbic acid, Saccharomyces cerevisiae and Zygosaccharomyces bailii cells accumulate the
H Pettersson et al.
Biochimica et biophysica acta, 1549(2), 155-160 (2001-11-03)
The mechanistic implications of the kinetic behaviour of a fusion protein of beta-galactosidase and galactose dehydrogenase have been analysed in view of predictions based on experimentally determined kinetic parameter values for the galactosidase and dehydrogenase activities of the protein. The
C F Mazitsos et al.
Journal of chromatography. A, 1029(1-2), 103-112 (2004-03-23)
Two chimaeric galactosyl-mimodye ligands were designed and applied to the purification of Pseudomonas fluorescens galactose dehydrogenase (GaDH). The chimaeric affinity ligands comprised a triazine ring on which were anchored: (i) an anthraquinone moiety that pseudomimics the adenine part of NAD+
Virapong Prachayasittikul et al.
International journal of biological sciences, 2(1), 10-16 (2006-04-06)
A chimeric bifunctional enzyme composing of galactose dehydrogenase (galDH; from Pseudomonas fluorescens) and lactate dehydrogenase (LDH; from Bacillus stearothermophilus) was successfully constructed. The chimeric galDH/LDH possessed dual characteristics of both galactose dehydrogenase and lactate dehydrogenase activities while exhibiting hexameric rearrangement
Jaeyoun Kang et al.
Parasite (Paris, France), 23, 21-21 (2016-05-14)
The localization of carbohydrate terminals in Kudoa septempunctata ST3-infected muscle of olive flounder (Paralichthys olivaceus) was investigated using lectin histochemistry to determine the types of carbohydrate sugar residues expressed in Kudoa spores. Twenty-one lectins were examined, i.e., N-acetylglucosamine (s-WGA, WGA
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