Chimeric mouse human IgG3 antibodies with an IgG4-like hinge region induce complement-mediated lysis more efficiently than IgG3 with normal hinge.

@article{Norderhaug1991ChimericMH,
  title={Chimeric mouse human IgG3 antibodies with an IgG4-like hinge region induce complement-mediated lysis more efficiently than IgG3 with normal hinge.},
  author={Lars Norderhaug and Ole Henrik Brekke and Bj{\o}rn Bremnes and Randi H Sandin and Audun Aase and T E Michaelsen and Inger Sandlie},
  journal={European journal of immunology},
  year={1991},
  volume={21 10},
  pages={
          2379-84
        }
}
We have altered the amino acid sequence of the hinge and the first constant domain (CH1) of mouse/human chimeric IgG3 antibodies by site-directed mutagenesis, so as to make the sequences identical to those of IgG4. All the mutant antibodies with altered hinge region were more active in complement activation and complement-mediated lysis than native IgG3. The mutations in CH1, however, did not alter the activity. This demonstrates the importance of the hinge region in modulating this effector… CONTINUE READING
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