The binding and uptake of ceruloplasmin was studied with rat liver cells using gold-labeled probes. Ceruloplasmins from either rat or sheep were used, in which different molecular conformations had been induced according to established biochemical criteria. The native protein from either species could bind not only to the endothelium, but also to Kupffer cells, at variance with previous findings. The proteins which had been converted to the conformation typical of stored molecules--which can be considered aged, but not denatured, according to standard activity and spectroscopic assays--were bound by endothelium irrespective of species, while only rat ceruloplasmin was able to bind to rat Kupffer cells. Internalization of sheep ceruloplasmin occurred with either endothelium or Kupffer cells. This property was lost with isolated suspended Kupffer cells. These findings suggest the presence of receptors for ceruloplasmin on Kupffer cells which are different from those present on endothelial cells.