PubMed:26231571
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/26231571","sourcedb":"PubMed","sourceid":"26231571","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/26231571","text":"Purification and Initial Functions of Sex-Specific Storage Protein 2 in Bombyx mori.\nIn this study, we identified a heat-resistant protein from the chrysalis stage of the silkworm which we named sex-specific storage protein 2 (SSP2). This protein was stable even at 80 °C, and has an amino acid sequence that is 90.65 % homologous to SP2. We utilized the heat-resistant characteristics of SSP2 to purify the protein and maintain its biological activity. In addition, using flow cytometry and the MTT assay, we found that SSP2 had anti-apoptotic effects on BmN cells, and that SSP2 could also inhibit cell apoptosis induced by chemical factors. These results suggest that SSP2 has a cell-protective function, and provides a basis for future work on the function of storage proteins in 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