Copper-containing plasma protein ceruloplasmin (Cp) forms a complex with lactoferrin (Lf), an iron-binding protein, and with the heme-containing myeloperoxidase (Mpo). In case of inflammation Lf and Mpo are secreted from the granules of neutrophils. Among the plasma proteins Cp seems to be the preferential partner of Lf and Mpo. After an intraperitoneal injection of Lf to rodents the “Cp-Lf” complex has been shown to appear in their bloodstream. Cp prevents the interaction of Lf with protoplasts of Micrococcus luteus. Upon immunoprecipitation of Cp the blood plasma becomes depleted of Lf and in dose-dependent manner loses the capacity to inhibit the peroxidase activity of Mpo, but not the Mpo-catalyzed oxidation of thiocyanate in the (pseudo)halogenating cycle. Antimicrobial effect against E.coli displayed by a synergistic system that includes Lf and Mpo-H2O2-chloride, but not thiocyanate, as the substrate for Mpo is abrogated when Cp is added. Hence, Cp can be regarded as an anti-inflammatory factor that res