Lipophorin (Lp) is the main haemolymphatic lipoprotein in insects and transports lipids between different organs. In adult females, lipophorin delivers lipids to growing oocytes. In this study, the interaction of this lipoprotein with the ovaries of
Rhodnius prolixus
was characterised using an oocyte membrane preparation and purified radiolabelled Lp (
125I-Lp). Lp-specific binding to the oocyte membrane reached equilibrium after 40-60 min and when
125I-Lp was incubated with increasing amounts of membrane protein, corresponding increases in Lp binding were observed. The specific binding of Lp to the membrane preparation was a saturable process, with a K
d of 7.1 ± 0.9 x 10
-8 M and a maximal binding capacity of 430 ± 40 ng
125I-Lp/μg of membrane protein. The binding was calcium independent and pH sensitive, reaching its maximum at pH 5.2-5.7. Suramin inhibited the binding interaction between Lp and the oocyte membranes, which was completely abolished at 0.5 mM suramin. The oocyte membrane preparation from
R. prolixus also showed binding to Lp from
Manduca sexta
. When Lp was fluorescently labelled and injected into vitellogenic females, the level of Lp-oocyte binding was much higher in females that were fed whole blood than in those fed blood plasma.
