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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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32
Produits recommandés
Conjugué
(N-linked)
Niveau de qualité
Forme
buffered aqueous glycerol solution
Concentration
≥0.05 unit/mL
Température de stockage
−20°C
Catégories apparentées
Description générale
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.
Actions biochimiques/physiologiques
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.
Définition de l'unité
One unit will hydrolyze 1.0 μmole of ovalbumin glycopeptide per min at pH 5.0 at 37°C.
Forme physique
Solution in 50% glycerol containing 50 mM citrate-phosphate buffer, pH 5.0, and BSA.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
No data available
Point d'éclair (°C)
No data available
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Les clients ont également consulté
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)
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
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
Anna C Need et al.
Journal of medical genetics, 49(6), 353-361 (2012-05-15)
There is considerable interest in the use of next-generation sequencing to help diagnose unidentified genetic conditions, but it is difficult to predict the success rate in a clinical setting that includes patients with a broad range of phenotypic presentations. The
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