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  • Title: Susceptibilities of lactoferrin and transferrin to myeloperoxidase-dependent loss of iron-binding capacity.
    Author: Winterbourn CC, Molloy AL.
    Journal: Biochem J; 1988 Mar 01; 250(2):613-6. PubMed ID: 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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