Abstract: To investigate the molecular basis and regulatory mechanism of antennal development, structure and function of Bombyx mori, high resolution and twodimensional polyacrylamide gel electrophoresis followed by matrixassisted laser desorption ionization and time of flight mass spectrometry (MALDI-TOF/MS) was applied to analyze the total proteins in antennae and their expression difference between male and female moths. The ImageMaster 6.0 software was used to analyze the two-dimensional gel electrophoresis profiles. Approximately a total of 550 protein spots were detected in the antenna of silk moth, most of which were arranged from 14 to 70 kD with pI value 4-8. In the two-dimensional gel electrophoresis profiles of male and female antenna, 419 and 489 protein spots were detected, respectively, and the number of matched protein spots between male and female was 326. The matching rate was 71.81%. There were 34 protein spots which have different gray value but were distributed in both gel electrophoresis profiles of male and female antenna. Meanwhile, 9 and 20 specific protein spots were detected in gel electrophoresis profiles of female and male, respectively. Sixty-three protein spots were identified by MALDI-TOF/MS and five proteins were obtained, including imaginal disk growth factor, cuticular protein RR-1 motif 15, thiol peroxiredoxin, vacuolar ATPase B subunit and gasp precursor. These proteins are involved in cell proliferation, epidermis formation, the removal of H₂O₂ in vivo, building up of a H⁺ gradient, etc. These five proteins were expressed differentially between female and male antenna, and all had higher expression levels in male antenna than in female antenna. The results provide some basic data for the further research of antenna proteins of the silk moth.

Key words: Bombyx mori, antenna, proteomics, two-dimensional electrophoresis, MALDI-TOF/MS, mass spectrometry