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
Recommended Products
recombinant
expressed in E. coli
Quality Level
form
ammonium sulfate suspension
specific activity
≥50 units/mg protein (biuret)
shipped in
wet ice
storage temp.
2-8°C
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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)
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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
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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