Skip to Content
Merck
All Photos(1)

Documents

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

Sign Into View Organizational & Contract Pricing
All Photos(1)

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

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

storage temp.

2-8°C

Gene Information

Pseudomonas fluorescens ... gdh(533113295)

Looking for similar products? Visit Product Comparison Guide

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Takahiro Mieda et al.
Plant & cell physiology, 45(9), 1271-1279 (2004-10-29)
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
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)
T E Curey et al.
Analytical biochemistry, 293(2), 178-184 (2001-06-12)
We report the development of a sensor for rapidly and simultaneously measuring multiple sugars in aqueous samples. In this strategy, enzyme-based assays are localized within an array of individually addressable sites on a micromachined silicon chip. Microspheres derivatized with monosaccharide-specific
D Peltzer et al.
Free radical research, 31 Suppl, S181-S185 (2000-02-29)
Green and white variegated leaves of Coleus blumei, Benth. were separated into albino and green sections and used to determine the distribution of vitamin C and L-galactose dehydrogenase activity, an enzyme supposed to be involved in ascorbate metabolism, in heterotrophic
Stephan Gatzek et al.
The Plant journal : for cell and molecular biology, 30(5), 541-553 (2002-06-06)
l-Galactose dehydrogenase (l-GalDH), a novel enzyme that oxidizes l-Gal to l-galactono-1,4-lactone (l-GalL), has been purified from pea seedlings and cloned from Arabidopsis thaliana. l-GalL is a proposed substrate for ascorbate biosynthesis in plants, therefore the function of l-GalDH in ascorbate
View All Related Papers

Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service