G0535
Glycopeptidase A from almonds
buffered aqueous glycerol solution, ≥0.05 unit/mL
Sinónimos:
N-Glycosidase A, N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase, PNGase A
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32
Productos recomendados
conjugate
(N-linked)
Quality Level
form
buffered aqueous glycerol solution
concentration
≥0.05 unit/mL
storage temp.
−20°C
Categorías relacionadas
General description
Glycopeptidase found in almonds can be divided into three groups- A, B and C. the optimum pH value and the isoelectric point of glycopeptidase A is 6.0 and 7.7 respectively. It has a preference for glycopeptides with long chains. It is also capable of hydrolyzing intact glycoproteins such as, desialyted human transferrin, ovalbumin etc. These proteins cleave glycoproteins with asialocarbohydrate moieties at their β-aspartyl-glucosylamine linkages.
Application
Glycopeptidase A from almonds is used for deglycosylation. It catalyzes the removal of N-linked oligosaccharide chains and converts Asn residue to Asp.
Biochem/physiol Actions
Hydrolyzes an N4-(acetyl-β-D-glycosaminyl)asparagine in which the N-acetyl-D-glucosamine residue may be further glycosylated, yielding a (substituted) N-acetyl-β-D-glucoaminylamine and the peptide containing an aspartic residue.
Unit Definition
One unit will hydrolyze 1.0 μmole of ovalbumin glycopeptide per min at pH 5.0 at 37°C.
Physical form
Solution in 50% glycerol containing 50 mM citrate-phosphate buffer, pH 5.0, and BSA.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
No data available
flash_point_c
No data available
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The Journal of biological chemistry, 284(15), 9764-9769 (2009-02-13)
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Asparagine-linked oligosaccharides in human placenta and umbilical cord as demonstrated by almond glycopeptidase.
N Takahashi et al.
FEBS letters, 146(1), 139-142 (1982-09-06)
T Takahashi et al.
Biochimica et biophysica acta, 657(2), 457-467 (1981-02-13)
The glycopeptidase preparation that has been isolated from almond emulsin and acts on beta-aspartylglycosylamine linkages in glycopeptides was separated into three active fractions by DEAE-cellulose column chromatography. The three discrete species of glycopeptidase (Groups A, B and C) have been
R P Miller et al.
Biochimica et biophysica acta, 954(1), 50-57 (1988-04-28)
The beta-subunit of dog kidney (Na+ + K+)-ATPase is a sialoglycoprotein and contains three potential N-glycosylation sites. In this study, the oligosaccharide chains of purified dog kidney beta-subunit were labeled with tritium by oxidation with sodium periodate or galactose oxidase
Amelie Croset et al.
Journal of biotechnology, 161(3), 336-348 (2012-07-21)
Glycosylation is one of the most common posttranslational modifications of proteins. It has important roles for protein structure, stability and functions. In vivo the glycostructures influence pharmacokinetics and immunogenecity. It is well known that significant differences in glycosylation and glycostructures
Artículos
N-Linked Glycan Strategies; Sigma-Aldrich.com
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