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. 1988 Mar 1;250(2):613–616. doi: 10.1042/bj2500613

Susceptibilities of lactoferrin and transferrin to myeloperoxidase-dependent loss of iron-binding capacity.

C C Winterbourn 1, A L Molloy 1
PMCID: PMC1148898  PMID: 2833250

Abstract

Apolactoferrin and apotransferrin lost their ability to subsequently bind iron when exposed to an excess of either HOCl or myeloperoxidase plus H2O2 and Cl-. Apolactoferrin, however, was more resistant than apotransferrin. By oxidizing a mixture of the two proteins, then separating them by immunoprecipitation, the difference in susceptibility was shown to be due to the greater reactivity of transferrin iron-binding groups, rather than protective groups on the lactoferrin molecule. The iron-saturated proteins were much more resistant to oxidative modification than the apoproteins. The greater resistance of apolactoferrin should be advantageous for maintaining its iron binding capacity when co-released with myeloperoxidase and reactive oxygen species from stimulated neutrophils.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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