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G6637

Sigma-Aldrich

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

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

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.

Unit Definition

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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+
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)
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