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Sodium dodecyl sulphate polyacrylamide gradient gel electrophoresis (SDS-PAGE) was used to determine the protein profiles of two mulberry variety leaves: the cultivated Morus alba var. Morittiana and the wild one Morus laevigata and their effects on haemolymph and silkgland protein patterns in final larval instar of silkworm Bombyx mori L. Results showed some differences in the number and abundance of protein bands in the two studied mulberry variety leaves as they were 5 bands in Morus alba var. Morittiana ranged between (47.27344.47 kDa), while, were 10 bands in Morus laevigata leaves ranged between (17.79350.11 kDa). However there were close similarity in haemolymph and silkgland protein patterns of larvae fed on the both studied mulberry varieties, which registrad 12 protein band in haemolymph and 15 protein bands in silkgland of larvae fed on the two mulberry varities.

Protein Patterns of Silkworm Bombyx mori L. Fed on Leaves of Wild and Cultivated Mulberry Varieties