Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release.

@article{Day1992StudiesOT,
  title={Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release.},
  author={Catherine L Day and Kathryn M. Stowell and Edward N Baker and John W Tweedie},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 20},
  pages={13857-62}
}
The factors influencing iron binding and release by lactoferrin have been addressed by comparison of the native full length molecule (Lf) with the N-terminal half of human lactoferrin (LfN) produced from the cloned cDNA expressed in baby hamster kidney (BHK) cells. The coding sequences for LfN were inserted into the expression vector pNUT between the metallothionein promoter and the human growth hormone transcription termination sequences. Transformed BHK cells were grown in roller bottles… CONTINUE READING

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H. M. Baker, G. E. Norris, S. V. Rumhall, M. F. Cole, J. R. McGhee
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