G7673
α-Galactosidase I, Alkaline from Cucumis melo
Synonyme(s) :
α-D-Galactoside Galactohydrolase, Melibiase
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in E. coli
Essai
≥85% (SDS-PAGE)
Forme
lyophilized solid
Activité spécifique
≥20 units/mg protein
Poids mol.
apparent mol wt ~84 kDa by SDS-PAGE
Conditions d'expédition
wet ice
Température de stockage
−20°C
Description générale
Alkaline α-Galactosidase I is a glycoside hydrolase, separated from the extracts of melon fruits. The activity of this enzyme is found to increase during the early stages of ovary development and fruit set.[1]
Application
Alkaline α-Galactosidase I was used to assay enzyme activity with 2 mmp-nitrophenyl-α-d-galactoside as substrate at pH 6.5 to compare with the enzyme activity of α-Gal A isolated and purified from Sf-9 insect cells infected with a recombinant baculovirus encoding normal α-Gal A gene.[2]
Actions biochimiques/physiologiques
α-Galactosidase form I from melon may play a significant role in photoassimilate partitioning in sink tissue. The form I enzyme has a preferred activity with raffinose and significant activity with stachyose. A unique feature of this enzyme is that it exhibits weak product inhibition by galactose.
This enzyme shows a preference for raffinose and also activity with stachyose. Unlike other a-Galctosidases, this enyzme also shows weak inhibition by galactose.
Propriétés physiques
This enzyme exhibits maximal activity between 30-37°C. Activity declines above 40°C.
Définition de l'unité
One unit will hydrolyze 1.0 μmole of p-nitrophenyl α-D-galactoside to p-nitrophenol and D-galactose per minute at pH 7.8 at 30 °C.
Forme physique
The product is supplied as a lyophilized powder containing Tris-HCl buffer salts, DTT, EDTA, and NaCl.
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Organes cibles
Respiratory system
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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N Asano et al.
European journal of biochemistry, 267(13), 4179-4186 (2000-06-24)
Fabry disease is a lysosomal storage disorder caused by deficient lysosomal alpha-galactosidase A (alpha-Gal A) activity. Deficiency of the enzyme activity results in progressive deposition of neutral glycosphingolipids with terminal alpha-galactosyl residue in vascular endothelial cells. We recently proposed a
Gao et al.
Plant physiology, 119(3), 979-988 (1999-03-09)
The cucurbits translocate the galactosyl-sucrose oligosaccharides raffinose and stachyose, therefore, alpha-galactosidase (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) is expected to function as the initial enzyme of photoassimilate catabolism. However, the previously described alkaline alpha-galactosidase is specific for the tetrasaccharide stachyose, leaving raffinose
Nir Carmi et al.
The Plant journal : for cell and molecular biology, 33(1), 97-106 (2003-08-29)
Raffinose and stachyose are ubiquitous galactosyl-sucrose oligosaccharides in the plant kingdom which play major roles, second only to sucrose, in photoassimilate translocation and seed carbohydrate storage. These sugars are initially metabolised by alpha-galactosidases (alpha-gal). We report the cloning and functional
Thomas Clavel et al.
Archives of microbiology, 195(1), 43-49 (2012-10-12)
We report the characterization of one novel bacterium, strain ERD01G(T), isolated from the cecum of a TNF(deltaARE) mouse. The strain was found to belong to the genus Streptococcus based on phylogenetic analysis of partial 16S rRNA gene sequences. The bacterial
M Benelmekki et al.
Colloids and surfaces. B, Biointerfaces, 101, 370-375 (2012-09-27)
Biomagnetic immobilization of histidine-rich proteins based on the single-step affinity adsorption of transition metal ions continues to be a suitable practice as a cost effective and a up scaled alternative to the to multiple-step chromatographic separations. In our previous work
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