G0535
Glycopeptidase A from almonds
buffered aqueous glycerol solution, ≥0.05 unit/mL
Synonyme(s) :
N-Glycosidase A, N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase, PNGase A
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
Concentration:
≥0.05 unit/mL
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Laissez-nous vous aiderconjugate
(N-linked)
form
buffered aqueous glycerol solution
concentration
≥0.05 unit/mL
storage temp.
−20°C
Quality Level
Catégories apparentées
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.
Classe de stockage
10 - Combustible liquids
wgk
WGK 1
flash_point_f
No data available
flash_point_c
No data available
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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
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)
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
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
Hui Zhou et al.
Analytical biochemistry, 427(1), 33-35 (2012-04-21)
Common de-N-glycosylation protocols usually require a lengthy incubation time. Although pressure cycling technology or scientific microwave reactors can accelerate this enzyme reaction, they may not be easily accessible. In this brief report, we employed an alternative strategy using a standard
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