蚕蛹中天然性别储存蛋白2的分离纯化和功能的初步探索
he purification and initial exploring functions of natural sex-special storage protein2 in pupa
20世纪80年代初,日本科学家在家蚕中发现了一类与家蚕的性别调控有关的储存蛋白,这种储存蛋白又分为储存蛋白1(SP1)和储存蛋白2(SP2)。本实验在蚕蛹中发现了一种耐80℃高温的性别储存蛋白2(SSP2),与SP2的氨基酸同源性高达90.65%的蛋白,根据蛋白本身的耐热性质,通过加热、离心、过滤等方法,再通过30%硫酸铵沉淀、Superdex 200、Resource Q等纯化手段,得到纯度较高并仍保持其生物活性的天然蛋白。利用流式细胞仪并结合MTT法检测SSP2对细胞的作用,发现SSP2对BmN细胞具有抗凋亡作用,并且SSP2对由于化学因素引起的细胞凋亡可能也具有一定的抗凋亡作用,因此我们推测,SSP2对细胞可能还具有一定程度的保护作用,为今后家蚕储存类蛋白的功能研究提供了依据。
1980s, Japanese scientists discovered a class of storage proteins in silkworm, which related with sex regulation, and the storage proteins are divided into such storage protein 1 (SP1) and storage protein 2 (SP2).In this study, we has found a heat-resistant protein named sex-specific storage protein 2 (SSP2) in chrysalis, it could resistance 80 ℃ temperature, and its amino acid homology with SP2 up to 90.65%. According to the heat-resistant characteristic of the SSP2, obtaining high purity and still maintain their biological activity of natural SSP2, by heating, centrifugation, filtration, and some way, and through the 30% ammonium sulfate precipitation, Superdex 200, Resource Q other purification methods. The combination of flow cytometry and MTT assay, it found that SSP2 on BmN cells with anti-apoptotic effects, and SSP2 could inhibite the cell apoptosis induced by chemical factors, so we speculated, SSP2 may could protect for cells, providing a basis for studying the function of storage protein in silkworm.
陈昊、张耀洲、舒特俊、叶曼、陈剑清
生物化学细胞生物学昆虫学
分子生物学蚕蛹性别储存蛋白2纯化功能分析
Molecular biologyPupaSex-specific storage-protein 2PurificationFunctional assay.
陈昊,张耀洲,舒特俊,叶曼,陈剑清.蚕蛹中天然性别储存蛋白2的分离纯化和功能的初步探索[EB/OL].(2012-02-27)[2025-08-22].http://www.paper.edu.cn/releasepaper/content/201202-1008.点此复制
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