Circulating half-life of PEGylated recombinant methioninase holoenzyme is highly dose dependent on cofactor pyridoxal-5'-phosphate.

@article{Yang2004CirculatingHO,
  title={Circulating half-life of PEGylated recombinant methioninase holoenzyme is highly dose dependent on cofactor pyridoxal-5'-phosphate.},
  author={Zhijian Yang and Xinghua Sun and Shukuan Li and Yuying Tan and Xiaoen Wang and Nan Zhang and Shigeo Yagi and Tomoaki Takakura and Yoshinao Kobayashi and Akio Takimoto and Takayuki Yoshioka and Akinori Suginaka and Eugene P. Frenkel and Robert M Hoffman},
  journal={Cancer research},
  year={2004},
  volume={64 16},
  pages={5775-8}
}
Recombinant methioninase (rMETase) has been shown to target the elevated methionine (MET) dependence of tumor cells and arrest their growth as well as make tumors more sensitive to standard chemotherapy agents. Polyethylene glycol (PEG)-modified rMETase (PEG-rMETase) has reduced antigenicity compared with unmodified rMETase. However, PEG-rMETase has a limited active circulating half-life due to rapid in vivo dissociation of its cofactor pyridoxal-5'-phosphate (PLP), a surprising finding… CONTINUE READING
2 Citations
29 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 29 references

Similar Papers

Loading similar papers…