Beta-M-acetylglucosaminidase

- Overview
  - 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 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. 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.
    
    Contents:
    N-acetylglucosaminidase in 20 mM Tris-HCl, 25 mM NaCl, pH 7.5
    5x Reaction Buffer 250 mM sodium phosphate, pH 5.0
    
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    Glycosidases
- Properties
  - Name
    
    β-N-acetylglucosaminidase, N-acetyl-β-d-glycosaminide N-acetylglucosaminohydrolase, glucosaminidase, hexosaminidase
    
    Purification
    
    Each lot of N-acetylglucosaminidase is tested for contaminating protease as follows; 10 µg of denatured BSA is incubated for 24 hours with 2 µL of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation.
    
    Storage
    
    Store enzyme at 4°C.
    
    Note
    
    Stable at least 12 months when stored properly. Several days exposure to ambient temperatures will not reduce activity.
    
    Activity
    
    >50 U/mL
    
    More Information
    
    Database Link
    
    EC 3.2.1.52
    
    * For research use only
- Applications
  - Application
    
    Glycan Release
- Reference
  - 1. Clarke, V. A., N. Platt and T.D. Betters. Cloning and expression of the beta-N-acetylglucosaminidase gene from Steptococcus pneumoniae. Generation of truncated enzymes with modified aglyconn specificity. J Biol Chem 270:8805-8814 (1995).
    2. Dwek, R. A., C. J. Edge, D. J. Harvey, M. R. Wormald and R. B. Parekh. Analysis of glycoprotein-associated oligosaccharides. Ann Rev Biochem 62: 65-100 (1993).
    3. Glasgow, L.R., J.C. Paulson and R.L. Hill. Systematic purification of five glycosidases from Streptococcus pneumoniae J Biol Chem 252:8615-8623(1977).
    4. Kobata, A. Use of endo- and exoglycosidases for structural studies of glycoconjugates. Anal Biochem 100: 1-14 (1979).
    5. Prime, S., J. Dearnley , A. M. Venton, R. B. Parekh and C. J. Edge. Oligosaccharide sequencing based on exo- and endoglycosidase digestion and liquid chromatographic analysis of the products. J Chromatogr A 720: 263-274 (1996).

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CofA

MSDS

Beta-M-acetylglucosaminidase

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