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

a)小铜蝶（Lycaena phlaeas daimio）蛹呈米色/黑色多态，其发育受成虫季节多态（春夏两季）发育的光周期和幼虫期给定温度的控制。即在长日照和短日照条件下发育的米色型和黑色型蛹分别倾向于发育中褐翅和红翅成虫。另外，在4℃冷藏5 d后，有很大比例的长日pharate蛹发育成头胸复合体和腹部分别为黑色和中间型的蛹。家蚕夏季形态产生激素（SMPH）初级结构的分析用0.9% NaCl对家蚕的脑-食管神经节复合物进行解剖，得到了1000个泡沫状的脑-食管神经节复合物。一种在亚洲逗号蝴蝶中显示smph活性的脑神经肽。采用凝胶过滤法和反相高效液相色谱法对smph活性肽粗提物进行纯化。两次获得吸光度在220nm处呈波浪状峰的肽段，并分析了smph活性肽n端氨基酸序列。结果，我们成功地从肽的n端得到了10个氨基酸的排列。然而，第一次和第二次试验获得的n端氨基酸序列有部分不同。我们应该尝试从家蚕的Br-SG配合物中纯化smph活性肽主体，并分析其n端氨基酸序列

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