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In an earlier report, we described the gene encoding a lipophorin receptor (LpR) of the silkworm, Bombyx mori L. (Lepidoptera: Bombycidae), and recombinant expression of the protein. The present study was performed to characterize the corresponding native BmLpR and its binding characteristics. Polyclonal anti-LpR antibody prepared against the cloned receptor fragment from the cytoplasmic domain specifically detected the receptor. Through immunoblotting, ovary and brain membrane protein samples of BmLpR have shown an apparent molecular mass of 105 kDa and 120 kDa under nonreducing and reducing conditions, respectively. Ligand binding of LpR supported the immunoblot results. It bound to high density lipophorin (HDLp) and has shown requirement of Ca2 in binding. Further, a dose-dependent inhibition by EDTA was observed in receptor ligand binding. The characteristics of the BmLpR protein confirm the properties of a ligand-receptor interaction similar to that of vertebrate low density lipoprotein receptor (LDLR).