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A bovine IgG heavy chain contains N-acetylgalactosaminylated N-linked sugar chains
N Aoki1, K Furukawa, K Iwatsuki
1Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University, Japan.
A 56K protein co-purified with bovine milk fat globule membrane (MFGM) proteins bound to Wisteria floribunda agglutinin (WFA) like most MFGM glycoproteins. Treatment with N-glycanase or beta-N-acetylhexosaminidase abolished the lectin binding to the protein. Amino acid sequence and immunoblot analyses revealed that the 56K protein is an IgG heavy chain. Lectin column chromatography of the oligosaccharides released by hydrazinolysis from the purified IgG heavy chains revealed that 0.08% of the total N-linked sugar chains bind to a WFA-agarose column, suggesting that they contain the beta-N-acetylgalactosaminylated structure.
A 56K protein co-purified with bovine milk fat globule membrane (MFGM) proteins bound to Wisteria floribunda agglutinin (WFA) like most MFGM glycoproteins. Treatment with N-glycanase or beta-N-acetylhexosaminidase abolished the lectin binding to the protein. Amino acid sequence and immunoblot analyses revealed that the 56K protein is an IgG heavy chain. Lectin column chromatography of the oligosaccharides released by hydrazinolysis from the purified IgG heavy chains revealed that 0.08% of the total N-linked sugar chains bind to a WFA-agarose column, suggesting that they contain the beta-N-acetylgalactosaminylated structure.