title: Essential metal ions alter the lactoferrin binding to the erythrocyte plasma membrane receptors.
abstract: The effect of metal ions at a concentration of 10(-8) to 10(-5) M [using their salts: ZnCl2, CdCl2, LiCl, CuSO4, NiSO4, Al2(SO4)3, (NH4)2MoO4 on the lactoferrin (Lf) binding to the erythrocyte membrane receptors was studied. In the absence of metal ions, Scatchard's analysis showed the existence of two kinds of binding site: one with high affinity and low capacity, and the another with low affinity and high capacity. All these metals, excluding Zn2+ and Cd2+, at a concentration 10(-5) M decreased the affinity of Lf binding (Ka1) to the high-affinity receptors. In the presence of Zn2+ and Cd2+, only the low-affinity binding site was found. Significant inhibition on the affinity (Ka2) of the low-affinity class of receptors showed Zn2+, Al3+, and Mo6+. Depending on their concentration (10(-8)-10(-5) M), these ions enhanced to a different extent, the binding capacity of the both types receptors, but the effect did not correspond to the applied doses. Several explanations of the mechanism for influence of the metal ions on the Lf-receptor interaction is discussed.
authors: Department of Biochemistry, Medical University of Sofia, Medical Faculty, Bulgaria.
authors: B
authors: B
authors: Taleva
authors: A
authors: A
authors: Maneva
authors: L
authors: L
authors: Sirakov
mesh_terms: D001692:Biological Transport; D004305:Dose-Response Relationship, Drug; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D007781:Lactoferrin / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology*; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000378:metabolism
chemical_list: D008670:Metals; D011956:Receptors, Cell Surface; D007781:Lactoferrin