2003Unpublished venueRequires access

The protein spectrum changes of two silkworm (Bombyx mori L.)hybrids during the development

Pavel Hyršl, Vladimír Šimek

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Abstract

The aim of this study was to analyse the protein spectrum of the haemolymph of the silkworm (Bombyx mori L., Lepidoptera, Bombycidae) during the development. We used two monovoltine bulgarian hybrids (Super1 x Vratza 35)x(Tv x Merefa2) and AS x KK. The haemolymph samples were collected every day of the last (5th) larval instar (8 days) and in the stage of prepupa and pupa. The samples were subjected to polyacrylamide gradient gel electrophoresis (SDS-PAGGE) and protein molecular weight was determined (Molecular Analyst software). We found 16 - 23 protein fractions in the range of 6.5 200 kDa. The main observed protein groups were: 200 kDa lipophorin, storage proteins in the range of 80 kDa and 30 kDa polypeptides. We demonstrated significant quantitative and qualitative changes in the haemolymph protein spectrum during development (continuous increase in the level of 30 kDa polypeptides and storage proteins during 5th instar) as well as differences in protein spectrum between males and females. No significant differences in protein spectrum were apparent between the two hybrids.

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The aim of this study was to analyse the protein spectrum of the haemolymph of the silkworm (Bombyx mori L., Lepidoptera, Bombycidae) during the development. We used two monovoltine bulgarian hybrids (Super1 x Vratza 35)x(Tv x Merefa2) and AS x KK. The haemolymph samples were collected every day of the last (5th) larval instar (8 days) and in the stage of prepupa and pupa. The samples were subjected to polyacrylamide gradient gel electrophoresis (SDS-PAGGE) and protein molecular weight was determined (Molecular Analyst software). We found 16 - 23 protein fractions in the range of 6.5 200 kDa. The main observed protein groups were: 200 kDa lipophorin, storage proteins in the range of 80 kDa and 30 kDa polypeptides. We demonstrated significant quantitative and qualitative changes in the haemolymph protein spectrum during development (continuous increase in the level of 30 kDa polypeptides and storage proteins during 5th instar) as well as differences in protein spectrum between males and females. No significant differences in protein spectrum were apparent between the two hybrids.

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Available abstract

The aim of this study was to analyse the protein spectrum of the haemolymph of the silkworm (Bombyx mori L., Lepidoptera, Bombycidae) during the development. We used two monovoltine bulgarian hybrids (Super1 x Vratza 35)x(Tv x Merefa2) and AS x KK. The haemolymph samples were collected every day of the last (5th) larval instar (8 days) and in the stage of prepupa and pupa. The samples were subjected to polyacrylamide gradient gel electrophoresis (SDS-PAGGE) and protein molecular weight was determined (Molecular Analyst software). We found 16 - 23 protein fractions in the range of 6.5 200 kDa. The main observed protein groups were: 200 kDa lipophorin, storage proteins in the range of 80 kDa and 30 kDa polypeptides. We demonstrated significant quantitative and qualitative changes in the haemolymph protein spectrum during development (continuous increase in the level of 30 kDa polypeptides and storage proteins during 5th instar) as well as differences in protein spectrum between males and females. No significant differences in protein spectrum were apparent between the two hybrids.

Key concepts: Bombyx mori, Hemolymph, Bombycidae, Instar, Lepidoptera genitalia, Polyacrylamide gel electrophoresis, Biology, Pupa

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