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Merck

G7673

Sigma-Aldrich

α-Galactosidase I, Alkaline from Cucumis melo

Synonym(e):

α-D-Galactoside Galactohydrolase, Melibiase

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About This Item

CAS-Nummer:
EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in E. coli

Assay

≥85% (SDS-PAGE)

Form

lyophilized solid

Spezifische Aktivität

≥20 units/mg protein

Mol-Gew.

apparent mol wt ~84 kDa by SDS-PAGE

Versandbedingung

wet ice

Lagertemp.

−20°C

Allgemeine Beschreibung

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.

Anwendung

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.

Biochem./physiol. Wirkung

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.

Physikalische Eigenschaften

This enzyme exhibits maximal activity between 30-37°C. Activity declines above 40°C.

Einheitendefinition

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.

Physikalische Form

The product is supplied as a lyophilized powder containing Tris-HCl buffer salts, DTT, EDTA, and NaCl.

Piktogramme

Exclamation mark

Signalwort

Warning

Gefahreneinstufungen

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°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
Aritz Pérez Ruiz de Garibay et al.
Drug design, development and therapy, 6, 303-310 (2012-11-03)
Gene-mediated enzyme replacement is a reasonable and highly promising approach for the treatment of Fabry disease (FD). The objective of the present study was to demonstrate the potential applications of solid lipid nanoparticle (SLN)-based nonviral vectors for the treatment of
Antonio Pisani et al.
Molecular genetics and metabolism, 107(3), 267-275 (2012-09-12)
Anderson-Fabry disease is an X-linked lysosomal storage disorder resulting from the deficiency of the hydrolytic enzyme alpha galactosidase A, with consequent accumulation of globotrioasoyl ceramide in cells and tissues of the body, resulting in a multi-system pathology including end organ

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