The effect of human serum transferrin and milk lactoferrin on hydroxyl radical formation from superoxide and hydrogen peroxide.
The effect of transferrins on hydroxyl radical formation from the superoxide anion and hydrogen peroxide generated by the xanthine-xanthine oxidase system has been studied by EPR using 5,5-dimethyl-1-pyrroline N-oxide as a spin trap. Neither diferriclactoferrin nor diferrictransferrin were found capable of promoting hydroxyl radical formation via the Haber-Weiss reaction even in the presence of EDTA in concentrations up to 1 mM. Activity observed by other authors may have been due to the presence of extraneous iron or an active protein impurity. Partially saturated transferrin and lactoferrin present in normal subjects may protect cells from damage by binding iron that might catalyze hydroxyl radical formation from superoxide and hydrogen peroxide. In any event, the hydroxyl radical formation observed in active neutrophils during phagocytosis cannot be associated with lactoferrin activity.
D001059:Apoproteins / Q000378:metabolism; D003676:Deferoxamine / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D005260:Female; D005609:Free Radicals; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006878:Hydroxides / Q000378:metabolism*; D017665:Hydroxyl Radical; D007700:Kinetics; D007781:Lactoferrin / Q000378:metabolism*; D007782:Lactoglobulins / Q000378:metabolism*; D008895:Milk, Human / Q000378:metabolism*; D004369:Pentetic Acid / Q000494:pharmacology; D011247:Pregnancy; D012710:Serum Albumin, Bovine / Q000494:pharmacology; D013481:Superoxides / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism*
D001059:Apoproteins; D005609:Free Radicals; D006878:Hydroxides; D007782:Lactoglobulins; D014168:Transferrin; D013481:Superoxides; D012710:Serum Albumin, Bovine; D017665:Hydroxyl Radical; D004369:Pentetic Acid; D006861:Hydrogen Peroxide; D007781:Lactoferrin; D003676:Deferoxamine