Analysis of the primary structure of summer-morph-producing hormone and photoperiodic and endocrine regulatory mechanism in the butterfly

a）小铜蝴蝶Lycaena phlaeas daimio具有蛹米色/黑色多态性，其发育被发现与成虫季节性多态性（春季和夏季形态）的发育明显相关，由幼虫阶段的光周期和温度控制。也就是说，在长日照和短日照条件下发育的米色和黑色类型的蛹分别倾向于发育成中音棕翅和红翅成虫。此外，大部分长日型蚤状体在4℃冷藏5d后，可发育为黑胸型蚤状体和中间型蚤状体。家蚕夏季形态产生激素（SMPH）的一级结构分析用0.9%NaCl溶液解剖家蚕，获得了泡沫状的千脑-食管神经节复合体。一种在亚洲斑蝶中显示SMPH活性的脑神经肽。SMPH活性肽粗提物经凝胶过滤和6步反相高效液相色谱纯化后，两次得到在220 nm处有一个吸收峰的肽段，并对SMPH活性肽N端氨基酸序列进行了分析。作为结果，我们成功地获得了10个氨基酸的排列从N-末端的肽。但第一次和第二次试验获得的N-末端氨基酸序列有部分差异。因此，我们有必要从家蚕Br-SG复合物中分离纯化SMPH活性肽，并对其N-端氨基酸序列进行分析

a) The small copper butterfly, Lycaena phlaeas daimio, has pupal beige/black polymorphism, development of which is found to be controlled in all apparent association with the development of adult seasonal polymorphism (spring and summer morphs) by photoperiod and temperature given in the larval stages. That is, pupae of beige and black types developed under long-day and short-day conditions tended to develop alto brown-winged and red-winged adults, respectively. In addition, a large proportion of long-day pharate pupae which had been chilled at 4℃ for 5 days developed into pupae whose head-thoracic complexes and abdomens were judged to be black and intermediate types, respectively. They developed into adults with more reddish wings as compared to those developed from the unchilled controlsb) Analysis of the primary structure of Bombyx summer-morph-producing hormone (SMPH) Foamy thousand brain-soboesophageal ganglion complexes were obtaind from the silkmoths, Bombyx mori, by dissection in 0.9% NaCl. A cerebral neuropeptide showing SMPH-activity in the Asian comma butterfly, Polygonia c-aureum. Crude extracts of SMPH-active peptide were purified by a gel-filtration and six steps of reverse-phased HPLC.A peptide fraction showing a suigle peak in absorbance of 220nm was obtained twice and analyzed amino acid sequence of N-terminal of the SMPH-active peptide. As the results, we succeeded to obtain the arrangement of 10 amino acids from the N-terminal of the peptides. However, amino acid sequences of N-terminals obtained by the first and second trials were different partly. We should try to purify the SMPH-active peptide main from Br-SG complexes of the silkmoth and analyze amino acid sequence of the N-terminals