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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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-837-4
MDL number:
EC 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
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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

Gene Information

Pseudomonas fluorescens ... gdh(533113295)

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)

Regulatory Information

常规特殊物品
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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
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
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+
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
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

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

以硫酸铵悬浮液形式提供的酶的使用指南

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