2003 Fiscal Year Final Research Report Summary
Analysis of the primary structure of summer-morph-producing hormone and photoperiodic and endocrine regulatory mechanism in the butterfly
| Project/Area Number |
14540628
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
動物生理・代謝
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| Research Institution | Yamaguchi University |
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Principal Investigator |
ENDO Katsuhiko Yamaguchi University, Fac.Sci., Physi., Biol.and Inform., Prof., 理学部, 教授 (70089845)
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| Co-Investigator(Kenkyū-buntansha) |
YAMANAKA Akira Yamaguchi University, Fac.Sci., Physi., Biol.and Inform., A.Prof., 理学部, 助教授 (20274152)
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| Project Period (FY) |
2002 – 2003
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| Keywords | Lycaena phlaeas / pupal body colors / seasonal morphs / Brain of the silkmoth / summer-morph hormone / purify and isolation / amino acid sequencce / primary structure |
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| Research Abstract |
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 controls
b) 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
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Research Products
(5 results)
