Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron- binding capacity

@article{Furmanski1989MultipleMF,
  title={Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron- binding capacity},
  author={Philip Furmanski and Z P Li and M B Fortuna and C V Swamy and Mahua Rani Das},
  journal={The Journal of Experimental Medicine},
  year={1989},
  volume={170},
  pages={415 - 429}
}
Lactoferrin (Lf), the major iron-binding component of milk, also a major constituent of the specific granules of neutrophils involved in antimicrobial activity and a glycoprotein thought to play a role in regulatory functions in the hematopoietic system as well as other physiologic activities, is shown to occur in three isoforms. One, Lf-alpha, binds iron; the other two, Lf-beta and Lf-gamma, express potent RNase activity, but do not bind iron. The three isoforms are very similar or identical… CONTINUE READING

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