Lipoprotein (a) (Lp(a)) and low-density lipoprotein (LDL) are structurally related to each other. Both exhibit identical phospholipid compositions and possess one molecule of apoprotein B-100 (apoB). Lp(a) contains, in addition, apoprotein (a) (apo(a)), which localizes to the particle surface and interacts with the apoB component by non-covalent and covalent forces. Protein-protein interaction is probably interrelated with protein-lipid interaction. Fluorescent analogs of phosphatidylcholine and sphingomyelin were inserted into the surface layer of LDL and Lp(a). The obtained fluorescence data reflecting mobility and distributional heterogeneity of the labeled lipids provided evidence that apoproteins discriminate between choline phospholipids and preferentially associate with phosphatidylcholine. This effect is enhanced in Lp(a) because of the presence of apolipoprotein (a). Higher affinity for Lp(a) as compared with LDL was also observed with a fluorescent diether analog of phosphatidylcholine in native serum. In contrast, the timedependent transfer of the same lipid into Lp(a) was slower compared with LDL, probably as a consequence of the more rigid surface of the former lipoprotein.