β -N-acetylglucosaminidase
β-N-acetylglucosaminidase (N-acetyl-β-d-glycosaminide N-acetylglucosaminohydrolase EC 3.2.1.30) 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 neighboring 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 (see Figure 1). 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.
50 U/ml - 3 U for 60 μL
GE31 data sheet pdf
