G0535
Glycopeptidase A from almonds
buffered aqueous glycerol solution, ≥0.05 unit/mL
Synonym(s):
N-Glycosidase A, N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase, PNGase A
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
Concentration:
≥0.05 unit/mL
conjugate
(N-linked)
Quality Level
form
buffered aqueous glycerol solution
concentration
≥0.05 unit/mL
storage temp.
−20°C
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.
Physical form
Solution in 50% glycerol containing 50 mM citrate-phosphate buffer, pH 5.0, and BSA.
Other Notes
One unit will hydrolyze 1.0 μmole of ovalbumin glycopeptide per min at pH 5.0 at 37°C.
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
No data available
flash_point_c
No data available
Regulatory Information
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Articles
Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.
Karen G Welinder et al.
The Journal of biological chemistry, 284(15), 9764-9769 (2009-02-13)
Proteome data of potato (Solanum tuberosum) tuber juice and of purified potato tuber vacuoles indicated that mature patatins may perhaps lack a C-terminal propeptide. We have confirmed this by complete mass spectrometric sequencing of a number of patatin variants as
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| G0535-.005UN | 04061833623992 |