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B-N-acetylglucosaminidase
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N-acetylglucosaminidase cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and glycoproteins. The cleavage rates of different linkages of GlcNAc on bi-, tri- and tetraantennary oligosaccharides is greatly dependent on the steric hindrance by neighbouring residues. The β(1-2)GlcNAc residue linked to the β(1-3)-linked mannose is cleaved at the highest rate and the β(1-2) GlcNAc residue linked to the β(1-6)-linked mannose at the lowest rate for all three oligosaccharides. The β(1-6) GlcNAc residue, when present, is removed at the second highest rate and the β(1-4) GlcNAc, third. On a triantennary structure, this residue is removed at the second highest rate. A bisecting β(1-4) GlcNAc linked to the β-linked mannose severely hinders cleavage of other GlcNAc residues–high concentrations of enzymes and prolonged incubation times are required for cleavage.
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1,2-O-Isopropylidene-β-L-idofuranuronic-6-13C acid γ-lactone
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1,2-O-Isopropylidene-β-L-idofuranuronic-1,6-13C2 acid γ-lactone
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1,2,3,6-Tetra-O-benzoyl-β-D-mannopyranose
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2,3,4,6-Tetra-O-acetyl-β-D-glucopyranosyl fluoride
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2-O-(2-Acetamido-2-deoxy-β-D-galactopyranosyl)-D-galactose
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Lactosylceramid
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4-Methylphenyl 4,6-O-benzylidene-1-thio-β-D-galactopyranoside
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4-Methylphenyl 2,3-di-O-benzyl-4,6-O-benzylidene-1-thio-α-D-mannopyranoside