The Research Of Colleterial Glands And Its Secretion In The Silkworm Moth

This paper mainly determines the content of adhesive proteins adhered to the eggsof Bombyx mori and the loose eggs sex-limited race(H-9)and comparisons of shape andsize of colleterial glands between different species (Qingsong×Haoyue,H-9,5B) arecarried on. At the same time ,the protein of 56 kD was separated ,purified and thesequence of the N-terminal amino were carried out. The results show that the contents of adhesive proteins adhered to the eggs ofBombyx mori(H-9) is about 0.022mg/egg, which is less than the normalspecies(Qingsong×Haoyue), Antherea pernyi and Actias selene Hubner which arerespectly 0.037 mg/egg,1.01 mg/egg and 1.1 mg/egg. In addition, we find the colleterialglands in the loose eggs sex-limited race (H-9, 5B) are smaller and lighter than thenormal and the content of its secretion is little. So there exists the trend of degradationin .the colleterial glands of deferent species in Bombyx mori. Judging from thecomparison between Bombyx mori, Antherea pernyi and Actias selene Hubner,the glandof Antherea pernyi is bigger than the others. The length of the reservoir of Anthereapernyi is 1.8 cm and Actias selene Hubner is 2.0 cm while Bombyx mori is 0.9 cm. Thearborescent regions of Antherea pernyi and Actias selene Hubner are more than Bombyxmori's . The SDS-PAGE analysis of the substance in the colleterial glands shows that theproteins included in Antherea pernyi whose molecular weight are 76 kD,72 kD, 56kD,30 kD,26 kD,24 kD,14 kD and 114 kD,92 kD,78 kD, 53 kD,50 kD,23 kD,12 kD in Actias selene Hubner. Compared with Bombyx mori (76 kD,68 kD,52 kD,48 kD,39 kD,26.5 kD,20.2 kD,18 kD,9.9 kD).Their molecular weight are bigger thanBombyx mori while less the types of proteins. in addition ,Microphotographs of femaleaccessory gland of Antheraea pernyi shows that there are circle cells and secretorygranules in the transection which is bigger than Bombyx mori's. The protein of 56 kD was purified successfully and is tried to be sequenced afterwestern-blotting of protein onto the PVDF by electrophresis. But the result is notsatisfied as we expected because of the quantity of protein ,human factors and otherreasons ,the N-terminal amino sequence of the protein is not be certified according to thefigure .because the protein is unknown to us ,it required to be further studied based onthe base of the research done before.