Effect of Carbethoxylation of Histidyl Residues in Bovine IgG2 on the Interaction with Staphylococcal Protein A

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  • SHIMAZAKI Keiichi
    Dairy Chemistry Laboratory, Department of Animal Science, Obihiro University of Agriculture and Veterinary Medicine
  • TSUCHIMOTO Tetsuya
    Dairy Chemistry Laboratory, Department of Animal Science, Obihiro University of Agriculture and Veterinary Medicine
  • SUKEGAWA Kinjiro
    Dairy Chemistry Laboratory, Department of Animal Science, Obihiro University of Agriculture and Veterinary Medicine

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Other Title
  • プロテインAとの相互作用におけるウシIgG 2のヒスチジン残基の寄与
  • プロテイン A ト ノ ソウゴ サヨウ ニ オケル ウシ IgG2 ノ ヒスチ

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Bovine IgG 2 showed adsorption to Protein A-Sepharose CL-4 B column but not IgG 1. Carbethoxylation of histidyl residues in IgG 2 by diethylpyrocarbonate resulted in the loss of its binding ability to Protein A. The number of histidyl residues carbethoxylated was 4.2 to 8.3 per IgG 2 molecule. Upon removal of the carbethoxyl groups by hydroxylamine, the IgG 2 molecule thus decarbethoxylated recovered its binding ability to Protein A. Therefore, it is concluded that histidyl residues in IgG 2 molecules is important for the interaction between IgG 2 and Protein A.

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