Potent anti-CD5 ricin A chain immunoconjugates from bacterially produced Fab' and F(ab')2.

@article{Better1993PotentAR,
  title={Potent anti-CD5 ricin A chain immunoconjugates from bacterially produced Fab' and F(ab')2.},
  author={Marco Better and Susan L. Bernhard and Suwen Lei and Dianne M. Fishwild and Julie A. Lane and Stephen F. Carroll and Arnold H. Horwitz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 2},
  pages={457-61}
}
We have used genetic engineering to obtain secretion of anti-human CD5 antibody fragments from Escherichia coli for conjugation to the 30-kDa form of ricin A chain (RTA30). This was accomplished by introducing stop codons at two positions in the hinge region of the human IgG1 gene so that coexpression of the truncated heavy-chain genes (Fd') with a light chain would result in Fab' and/or F(ab')2 proteins containing either one or two interheavy-chain cysteines. An Fd' gene encoding both… CONTINUE READING
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