抄録
Plasma proteins from the yellow-spotted longicorn beetle Psacothea hilaris were identified and their changes were surveyed during late larval development and the pupal stage. Three major proteins with different electrophoretic mobilities were observed in the hemolymph, which we tentatively named as plasma proteins I, II and III. Each protein showed characteristic fates during larval-pupal-adult development. Two-step purification of these proteins was achieved by using high-performance liquid chromatography (HPLC). The native molecular masses of I, II and III were estimated by gel filtration chromatography to be 340 kDa, 280 kDa and 260 kDa, respectively. The apoproteins of I, II and III consisted of identical subunits with 76 kDa, 74 kDa and 76 kDa, respectively. Psacothea-vitellogenin (female-specific plasma protein) appeared in the hemolymph 3 weeks after adult emergence. The native molecule of vitellogenin was about 400 kDa, and consisted of a heavy subunit (165 kDa) and a light one (40 kDa).
