| Enzyme Formulation | - Lyophilized powder containing citrate-phosphate buffer, pH 5.0.
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| Enzyme Source | - Almond. Enzyme also knows as Peptide N-Glycosidase A, Glycopeptidase from almonds, Almond glycoamidase, Peptide-N(4)-(N-acetyl- glucosaminyl) asparagine amidase.
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| Enzyme Specific Activity | - > 5 units/mg 5 units/mg —>
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| Enzyme Specificity | - PNGase A from almonds cleaves N-glycan chains linked to Asparagine from glycopeptides. The enzyme hydrolyzes an N(4)-(acetyl-ß D-glucosaminyl) asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-ß D-glucosaminylamine and a peptide containing an aspartate residue. The enzyme cleaves N-glycans with or without a(1,3)-linked core fucose residues present in insect and plant glycoproteins. This differs from PNGase F, which cannot remove N-glycans with a(1,3)-linked core fucose. PNGase A requires glycopeptides as substrates. Glycopeptides can be obtained by digesting the glycoprotein with trypsin [1,2] or pepsin. Does not act on (GlcNAc)-Asn, because it requires the presence of more than two amino acid residues in the substrate.
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| Enzyme Unit Definition | - One unit is defined as the amount of enzyme required to hydrolyze 1 mol ovalbumin glycopeptide per min at pH 5.0 and 37C.
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