Mutations of two lysine residues in the CDR loops of a recombinant immunotoxin that reduce its sensitivity to chemical derivatization.

@article{Benhar1994MutationsOT,
  title={Mutations of two lysine residues in the CDR loops of a recombinant immunotoxin that reduce its sensitivity to chemical derivatization.},
  author={Itai Benhar and Ulrich Brinkmann and Keith O. Webber and Ira Pastan},
  journal={Bioconjugate chemistry},
  year={1994},
  volume={5 4},
  pages={
          321-6
        }
}
B3(Fv)-PE38 is a recombinant single-chain immunotoxin in which the Fv region of monoclonal antibody B3 is connected to a truncated form of Pseudomonas exotoxin. It would be desirable to use the lysine residues of the molecule for chemical modification so that it can be derivatized with poly(ethylene glycol) to achieve reduced immunogenicity or with the Bolton-Hunter reagent for biodistribution studies. We found that derivatizing lysine residues of B3(Fv)-PE38 causes a marked loss of specific… CONTINUE READING
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