The specific accumulation and distribution of a storage protein -1 (SP-l) was found in the hemolymph and fat body during last instar larval and pupal stages of Heliocoverpa assulta. Throughout the density gradient ultracentrifugation and the serial chromatograpic applications, SP-l was purified. The molecular mass of its subunit was measured as 80 kDa. Western blotting showed that SP-l exists in fat body extract during late larval and pupal stages. With autoradiography, SP-l was found to be synthesized in the peripheral fat body of 5-day-old larvae, but not in perivisceral fat body of 1- day - old pupa. Ligand blotting with solubilized membrane protein in fat body extract showed a distinct SP-l receptor and its molecular mass was measured as 145 kDa. In vitro binding assay of $^{14}C$-labeled SP-l for solubilized membrane proteins had no significant competitiveness with another major hemolymph protein such as lipophorin. The binding of membrane with SP-l required $Ca^{2+}$ and showed optimal pH of 6.5.