Glycosylation of a VH residue of a monoclonal antibody against alpha (1- ---6) dextran increases its affinity for antigen

@article{Wallick1988GlycosylationOA,
  title={Glycosylation of a VH residue of a monoclonal antibody against alpha (1- ---6) dextran increases its affinity for antigen},
  author={S C Wallick and Elvin A. Kabat and Sherie L. Morrison},
  journal={The Journal of Experimental Medicine},
  year={1988},
  volume={168},
  pages={1099 - 1109}
}
We have observed that antidextran hybridomas with potential N-linked glycosylation sites in VH have higher affinity for polymeric dextran and for isomaltoheptaose than those lacking potential glycosylation sites. In these studies we have used gene transfection and expression techniques to verify that the carbohydrate addition sites in VH were used. The carbohydrate of the VH region was accessible for binding by the lectin Con A. By ELISA analysis it was demonstrated that the aKa of the antibody… CONTINUE READING

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