Se connecter pour consulter les tarifs organisationnels et contractuels.
Sélectionner une taille de conditionnement
A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-843-7
MDL number:
Specific activity:
≥30 units/mg solid
Biological source:
fungus (Dactylium dendroides)
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aiderService technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aiderNom du produit
Galactose Oxidase from Dactylium dendroides, ≥30 units/mg solid
biological source
fungus (Dactylium dendroides)
form
lyophilized
specific activity
≥30 units/mg solid
storage temp.
−20°C
Quality Level
Vous recherchez des produits similaires ? Visite Guide de comparaison des produits
Catégories apparentées
Application
Galactose Oxidase from Dactylium dendroides has been used as a component for galactose oxidase treatment of arabinogalactan. It has also been used to co-immobilise with peroxidase for the preparation of a biosensor for galactose detection.
Galactose oxidase may be used as an analytical tool for the specific determination of D-galactose in blood plasma, plant extracts, and phospholipids. It could be used for the characterization of terminal D-galactoside units in several polymers. It may also be useful in the determination of lactose.
Biochem/physiol Actions
Galactose oxidase catalyzes the coversion of D-galactose to D-galacto-hexodialdose.
2-Deoxy-D-galactose, lactose, melibiose, raffinose and stachyose react with galactose oxidase in the peroxidase:o-tolidine system.
Essentially no oxidation of D-glucose, L-galactose, L-arabinose or D-glucuronate has been observed.
2-Deoxy-D-galactose, lactose, melibiose, raffinose and stachyose react with galactose oxidase in the peroxidase:o-tolidine system.
Essentially no oxidation of D-glucose, L-galactose, L-arabinose or D-glucuronate has been observed.
Galactose oxidase has several applications in bioanalytics and histology. This free radical enzyme possess high substrate specificity.
The specificity for galactose and other sugars is similar to that described by Avigad.
General description
Galactose oxidase is a member of radicalcoupled copper oxidases family. It is a fungal secretory enzyme.
Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus Dactylium dendroides. It catalyzes the oxidation of a range of primary alcohols, including D-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide.
Other Notes
One unit will produce a ΔA425 of 1.0 per min at pH 6.0 at 25 °C, in a peroxidase and o-tolidine system. Reaction volume = 3.4 mL. Light path = 1 cm.
Physical form
Lyophilized, contains buffer salts and stabilizer
Preparation Note
Chromatographically purified
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Faites votre choix parmi les versions les plus récentes :
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Development of an immunoassay for larch arabinogalactan and its use in the detection of larch arabinogalactan in rat blood
Groman E V and Gou D
Carbohydrate Research, 301(1-2), 69-76 (1997)
Rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability
Tkac J, et al.
BioTechnology: An Indian Journal, 13(12), 931-936 (1999)
Biocatalytic desymmetrization of an atropisomer with both an enantioselective oxidase and ketoreductases.
Bo Yuan et al.
Angewandte Chemie (International ed. in English), 49(39), 7010-7013 (2010-08-18)
Development of a galactose biosensor with galactose oxidase-immobilized epidermis of Solanum lycopersicum: potential point-of-care testing for citrin deficiency in high-prevalence areas.
Hencher H C Lee et al.
Clinica chimica acta; international journal of clinical chemistry, 412(3-4), 391-392 (2010-10-26)
Grant E Henderson et al.
Bioconjugate chemistry, 22(5), 903-912 (2011-03-15)
The site-specific modification of proteins is expected to be an important capability for the synthesis of bioconjugates in the future. However, the traditional repertoire of reactions available for the direct modification of proteins suffers from lack of specificity, necessitating costly
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique