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Chemical Liberation of N-linked Oligosaccharides from Glycoproteins

  • Shin-ichi Nakakita

Abstract

When N-linked oligosaccharides are chemically liberated from the glycoproteins, the hydrazine anhydrous is generally used. Hydrazinolysis has been originally used as a method to determine carboxyl terminal amino acid of protein. Yoshizawa et al. (1966) found that the method is well applicable to chemical liberation of oligosaccharides from glycoproteins. Upon hydrazinolysis, lyophilized samples including glycoproteins are completely solved in hydrazine, and thus, the reaction proceeds smoothly. After hydrazinolysis, released acetyl group of amino sugars, such as GlcNAc and GalNAc, must be subjected to re-acetylation (Takasaki et al. 1982) (Fig. 1).

Keywords

Acetic Anhydride Amino Sugar Seal Tube Rotary Pump Enzymatic Procedure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. Takasaki S, Mizuochi T, Kobata A (1982) Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides. In: Ginsburg V (ed) Methods in enzymology, vol 83. Academic Press, New York, pp 263–268Google Scholar
  2. Yoshizawa Z, Sato T, Schmid K (1966) Hydrazinolysis of alpha-1-acid glycoprotein. Biochim Biophys Acta 121:417–420Google Scholar

Copyright information

© Springer 2008

Authors and Affiliations

  • Shin-ichi Nakakita
    • 1
  1. 1.Department of Functional Glycomics, Life Science Research CenterKagawa UnviersityKagawaJapan

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