C3b covalently bound to IgG demonstrates a reduced rate of inactivation by factors H and I

@article{Fries1984C3bCB,
  title={C3b covalently bound to IgG demonstrates a reduced rate of inactivation by factors H and I},
  author={Louis F. Fries and Thelma Gaither and Carl H. Hammer and Michael M. Frank},
  journal={The Journal of Experimental Medicine},
  year={1984},
  volume={160},
  pages={1640 - 1655}
}
We have prepared C3b covalently linked to IgG via a hydroxylamine-sensitive bond between the C3b alpha' chain and sites predominantly, but not exclusively, located in the IgG heavy chain. This C3b species displays relative resistance to inactivation by factors H and I when compared with free C3b. This resistance appears to be due entirely to reduced affinity of C3b-IgG for factor H. Resistance to inactivation is not conferred on C3b by binding to another serum glycoprotein of similar size… CONTINUE READING

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