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
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biological source
Pseudomonas fluorescens
Quality Level
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
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We have studied the enzymological properties of L-galactose dehydrogenase (l-GalDH), a key enzyme in the biosynthetic pathway of l-ascorbate (AsA) in plants. L-GalDH was purified approximately 560-fold from spinach leaves. The enzyme was a homodimer with a subunit mass of
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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
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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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