Molecular characteristics of lipophorin, the juvenile hormone‐binding protein in the hemolymph of the Colorado potato beetle

Lipophorin, the protein that specifically binds juvenile hormone in the hemolymph of the Colorado potato beetle, Leptinotarsa decemlineata, is a high‐density lipoprotein of Mr ∼ 574,000. Lipophorin contains 43% lipid and is composed of two apoproteins: apolipophorin I (Mr ∼ 251,000) and apolipophorin II (Mr ∼ 78,000). Both apoproteins contain mannose residues. Carotenoids make up a substantial part of the lipid fraction. Lipophorin constitutes about 25% of the total hemolymph proteins. Its concentration in the hemolymph (26 μM in 4‐day‐old long‐day and 40 μM in 4‐day‐old short‐day beetles) changes with different physiological conditions concomitant with changes in total protein content. Lipophorin specifically binds 10R‐juvenile hormone III with high affinity. The dissociation constant for 10R‐juvenile hormone III is 12 ± 2 nM. One lipophorin molecule contains one specific juvenile hormone‐binding site. The concentration of binding sites therefore equals that of lipophorin in hemolymph.