| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1982238 | Insect Biochemistry and Molecular Biology | 2012 | 8 Pages |
The 30K proteins comprise about 35% of the total embryo yolk proteins and function as storage proteins during embryonic development of the domesticated silkworm Bombyx mori. The most abundant components of hemolymph are 30K proteins in the early and middle pupal stages. In the present study, the 30K protein BmLP7 was purified from larval hemolymph by chromatography. We prepared the antibody of this protein and found that it could bind to both BmLP3 and BmLP7. We used western blotting to analyze the dynamic change of BmLP3 and BmLP7 proteins in the hemolymph during development and found their concentration decreased dramatically from day 4 pupae, which appears to be linked to their accumulation in the oocyte for forming yolk granule since then. We found BmLP3 and BmLP7 proteins reduced significantly in day 10 eggs (the day before hatching). The crude extract of the newly hatched larvae showed proteolytic activity against BmLP3 and BmLP7 and immunohistochemistry showed BmLP3 and BmLP7 were degraded in the embryonic gut lumen in day 10 eggs. These systematic studies of BmLP3 and BmLP7 reveal their synthesis, transportation and degradation, which could represent the experience of all 30K proteins.
Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (228 K)Download as PowerPoint slideHighlights► We found that the BmLP3 and BmLP7 proteins in the hemolymph were accumulated into the ovary after day 1 pupae. ► BmLP3 and BmLP7 proteins formed yolk granules and reduced significantly in day 10 eggs (the day before hatching). ► BmLP3 and BmLP7 proteins were ingested into the gut lumen of embryo and degraded by proteases before hatching. ► The systematic studies of BmLP3 and BmLP7 reveal their synthesis, transportation and degradation.
