Abstract: 【Objective】The protein composition of the egg development of the higher producing royal jelly bees (Apis mellifera L.) were investigated. 【Method】This pioneer study was to separate and quantify proteins of the eggs of the higher producing royal jelly worker bees (Apis mellifera L.) by using two-dimensional gel electrophoresis along with their three days development.【Result】The results showed that 160, 195 and 176 proteins with wide rang of molecular weight (17-80KDa) and relatively narrow scope of pI (4.00-8.40) could be detected on day1, day2 and day3 respectively during the developmental process of the egg. Meanwhile 44 protein spots were constantly detected along with the egg development, among them 36 percent were in up trend along with the egg development, 14 percent were in down trend along with the development of the egg, and 39 percent were of the largest expressed volume on day 2. In addition, the specific proteins were expressed on day 1, day 2 and day 3 (89, 77, 80 respectively). Besides the coexistent and specific proteins, 24 proteins were expressed on day 1 and day 2 but silenced on day 3, 49 proteins were expressed on day 2 and day 3 but silenced on day 1, only 3 proteins were expressed on day 1 and day 3 but silenced on day 2.【Conclusion】The result indicates that the egg development is a sequential and complex gene controlled process, while the eggs of day 2 express the most active. The coexistent proteins suggest that it is conservative and indispensable for this event. The specific proteins suggest that the different developmental stage need specific proteins to regulate.

Key words: honeybees, higher production royal jelly, worker bee’s egg, two-dimensional gel electrophoresis, proteome