G7673
α-Galactosidase I, Alkaline from Cucumis melo
Synonym(s):
α-D-Galactoside Galactohydrolase, Melibiase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥20 units/mg protein
Assay:
≥85% (SDS-PAGE)
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
assay
≥85% (SDS-PAGE)
form
lyophilized solid
specific activity
≥20 units/mg protein
mol wt
apparent mol wt ~84 kDa by SDS-PAGE
shipped in
wet ice
storage temp.
−20°C
General description
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.
This enzyme exhibits maximal activity between 30-37°C. Activity declines above 40°C.
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.
Biochem/physiol Actions
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.
Physical form
The product is supplied as a lyophilized powder containing Tris-HCl buffer salts, DTT, EDTA, and NaCl.
Other Notes
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.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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
Xiao-Liang Pan et al.
The journal of physical chemistry. B, 117(2), 484-489 (2012-12-20)
The enzyme α-galactosidase (α-GAL), a member of glycoside hydrolase family 27, catalyzes the removal of a nonreducing terminal α-galactose residue from polysaccharides, glycolipids, and glycopeptides. α-GAL is believed to have the double displacement retaining reaction mechanism. In this work, the
Junpei Zhou et al.
Journal of microbiology and biotechnology, 22(11), 1532-1539 (2012-11-06)
The α-galactosidase-coding gene agaAJB13 was cloned from Sphingomonas sp. JB13 showing 16S rDNA (1,343 bp) identities of < or =97.2% with other identified Sphingomonas strains. agaAJB13 (2,217 bp; 64.9% GC content) encodes a 738-residue polypeptide (AgaAJB13) with a calculated mass
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