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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
EC Number:
1.1.1.48 (BRENDA, IUBMB)
EC Number:
232-837-4
MDL number:
MFCD00130622
UNSPSC Code:
12352204
NACRES:
NA.54
Pricing and availability is not currently available.

biological source

Pseudomonas fluorescens

Quality Level

200

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

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1 of 4

This Item
10662046001L2011L1378
β-Galactose Dehydrogenase from Pseudomonas fluorescens recombinant, expressed in E. coli, ammonium sulfate suspension, ≥50 units/mg protein (biuret)

G6637

β-Galactose Dehydrogenase from Pseudomonas fluorescens

β-Galactose Dehydrogenase S suspension, ~80 units/mg protein (At 25 °C with galactose as the substrate.), pkg of 50 U

10662046001

β-Galactose Dehydrogenase S

D-Lactic Dehydrogenase from Lactobacillus leichmannii ammonium sulfate suspension, ≥250 units/mg protein (biuret)

L2011

D-Lactic Dehydrogenase from Lactobacillus leichmannii

L-Lactic Dehydrogenase from bovine muscle Type X, ammonium sulfate suspension, ≥600 units/mg protein

L1378

L-Lactic Dehydrogenase from bovine muscle

assay

0.5—2.0 mg protein/mL (biuret)

assay

-

assay

-

assay

3.0—25.0 mg protein/mL (biuret)

biological source

Pseudomonas fluorescens

biological source

-

biological source

-

biological source

bovine muscle

Gene Information

Pseudomonas fluorescens ... gdh(533113295)

Gene Information

-

Gene Information

-

Gene Information

cow ... LDHA(281274), LDHB(281275)

application(s)

life science and biopharma

application(s)

-

application(s)

-

application(s)

life science and biopharma

suitability

suitable for enzyme test

suitability

-

suitability

-

suitability

-

Application

β-Galactose Dehydrogenase from Pseudomonas fluorescens has been used for competitive inhibition in lectin histochemistry.[1][2] It has also been used to measure the hydrolysis activity of Haloferax alicantei β-galactosidase on different disaccharides.[3]

Biochem/physiol Actions

β-galactose dehydrogenase catalyzes the oxidation of β-D-galactose to D-galactono-gammalactone[4].

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

11 - Combustible Solids

wgk_germany

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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    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
    R D Hancock et al.
    FEMS microbiology letters, 186(2), 245-250 (2000-05-10)
    Saccharomyces cerevisiae cells incubated with D-glucose (D-Glc), D-galactose or D-mannose (D-Man) synthesised D-erythroascorbic acid (D-EAA) but not L-ascorbic acid (L-AA). Accumulation of D-EAA was observed in cells incubated with D-arabinose (D-Ara) whilst accumulation of L-AA occurred in cells incubated with
    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+
    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
    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
    View All Related Papers

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