论文部分内容阅读
为揭示云斑天牛(Batocera lineolata Chevrolat)对气味分子的识别机制,通过荧光结合试验和葡聚糖凝胶G75(Sephadex G75)层析研究了云斑天牛对气味分子的识别情况,并对云斑天牛气味结合蛋白进行了分离纯化。结果表明,云斑天牛气味结合蛋白能与荧光探针N-苯基-1-萘胺(N-phenyl-1-naphthylamine,1-NPN)产生荧光结合,云斑天牛触角部位的总蛋白提取液中存在pro.Ⅰ-Ⅻ(ProteinⅠ-Ⅻ)12种大分子粗提蛋白,这12种大分子粗提蛋白经Sephadex G75纯化后,得到1种能与荧光探针1-NPN产生荧光结合的纯化蛋白pur-pro.I(purified protein I)。纯化蛋白pur-pro.I分子质量约为15.2 ku,对应为大分子粗提蛋白pro.Ⅻ(ProteinⅫ)。鉴定认为,分离纯化蛋白pur-pro.I是云斑天牛的一种气味结合蛋白。
In order to reveal the recognition mechanism of Odor molecules by Batocera lineolata Chevrolat, the recognition of Odor molecules by Gastrodia elata was studied by fluorescence binding assay and Sephadex G75 chromatography. Cloud-day pest odor-binding proteins were isolated and purified. The results showed that the odor-binding protein of C. aeruginosa could be fluorescently combined with the fluorescent probe N-phenyl-1-naphthylamine (1-NPN). The total protein Twelve macromolecular crude extracts of pro.Ⅰ-Ⅻ (ProteinⅠ-Ⅻ) were isolated from the extract. The crude extracts of these twelve kinds of macromolecules were purified by Sephadex G75 to obtain one kind of fluorescent protein Purified protein pur-pro. I (purified protein I). Purified protein pur-pro.I molecular weight of about 15.2 ku, corresponding to the macromolecular crude protein pro.Ⅻ (ProteinⅫ). Identification that the purifying protein pur-pro.I is a smell-binding protein.