An analysis of hemolymph protein profiles during the finalinstar, prepupa and pupa of the silkworm, Bombyx mori(Lepidoptera: Bombycidae)

Sodium dodecyl sulphate ĄV polyacrylamide gradient gel electrophoresis (SDS-PAGGE) was used to determine the hemolymph protein profiles of the silkworm Bombyx mori during the development of the final instar, prepupa and pupa. Using this technique it was possible to distinguish approximately 16-23 protein fractions in the final instar larva, in the prepupa about 16-18 bands were detected and in pupae about 19 protein fractions were observed. Although the changes in protein profiles during development were initially qualitatively the same in both sexes, later, during larval-pupal transformation and development of pupae, a clear sexual dimorphism was observed. Female specific proteins (vitellogenin, approximately 178 kDa) appeared in the early pupal stage. In addition to well-defined protein fractions such as lipophorins (200ĄV217 kDa), storage proteins (70{80 kDa) and 30 kDa polypeptides, some undetermined protein fractions (PF1-PF7) varying from 18{128 kDa were also detected. Lysozyme content was also quantified during the developmental process using radial diffusion technique.