Journal of Protein Chemistry

, Volume 8, Issue 4, pp 519–528 | Cite as

Modification of galactose andN-acetylgalactosamine residues by oxidation of C-6 hydroxyls to the aldehydes followed by reductive amination: Model systems and antifreeze glycoproteins

  • David T. Osuga
  • Milton S. Feather
  • Mena J. Shah
  • Robert E. Feeney
Articles

Abstract

Amino acids and peptides have been attached to the C-6 hydroxyls of the galactose and the N-acetylgalactosamine by first oxidizing the C-6 hydroxyls to the aldehydes by galactose oxidase in the presence of small amounts of catalase, followed by reductive amination (α-amino group) in the presence of cyanoborohydride. The activity of oxidized antifreeze glycoprotein was >70% of the original, and considerable activity has been retained with some substitutions on reductive amination using cyanoborohydride. The following were some activities retained (as compared with the oxidized antifreeze glycoprotein): Gly, 64; (Gly)2, 88; (Gly)3, 82; (Gly)4, 70; Gly-Gly-NH2, 44, Gly-Glu, 13; Gly-Leu, 40; Gly-Tyr, 57; Gly-Gly-Leu, 50; Gly-Gly-Phe, 30; and Gly-Gly-Val, 35. On amino acid analysis of acid hydrolysates, some release of the amino acid attached by amination occurred; e.g., Gly-Tyr gave 0.26 Gly and 0.49 Tyr per disaccharide.

Key words

antifreeze glycoprotein galactose oxidase oxidation reductive amination of carbohydrates amination with peptides 

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Copyright information

© Plenum Publishing Corporation 1989

Authors and Affiliations

  • David T. Osuga
    • 1
  • Milton S. Feather
    • 1
  • Mena J. Shah
    • 1
  • Robert E. Feeney
    • 1
  1. 1.Department of Food Science and TechnologyUniversity of CaliforniaDavis
  2. 2.Department of BiochemistryUniversity of MissouriColumbia

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