Abstract
It is shown that cultured cells of the CV-1 line possess the capacity for high-affinity binding of ceruloplasmin, show a kinetics of saturation, and internalize ceruloplasmin. Propagation of cells in medium supplemented with fetal calf serum depleted of ceruloplasmin results in a two-fold increase of high-affinity receptor expression on the cell surface. This phenomenon is not accompanied by any change in the receptor-ligand affinity. Ceruloplasmin binding to the cell surface and subsequent internalization do not lead to its marked degradation.
Published Version
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