Efficient clearance of poly(ethylene glycol)-modified immunoenzyme with anti-PEG monoclonal antibody for prodrug cancer therapy.

@article{Cheng2000EfficientCO,
  title={Efficient clearance of poly(ethylene glycol)-modified immunoenzyme with anti-PEG monoclonal antibody for prodrug cancer therapy.},
  author={T L Cheng and B M Chen and J W Chern and Mengfeng F Wu and Steve R Roffler},
  journal={Bioconjugate chemistry},
  year={2000},
  volume={11 2},
  pages={258-66}
}
The F(ab')(2) fragment of the anti-TAG-72 antibody, B72.3, was covalently linked to Escherichia coli-derived beta-glucuronidase that was modified with methoxypoly(ethylene glycol). The conjugate (B72.3-betaG-PEG) localized to a peak concentration in LS174T xenografts within 48 h after injection, but enzyme activity persisted in plasma such that prodrug administration had to be delayed for at least 4 days to avoid systemic prodrug activation and associated toxicity. Conjugate levels in tumors… CONTINUE READING
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Studies with polymer enzyme conjugates and AMIRACS

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