{"title":"家蚕羽化激素的分离及氨基酸序列分析","authors":"Takaharu Kono , Hiromichi Nagasawa , Akira Isogai , Hajime Fugo , Akinori Suzuki","doi":"10.1016/0020-1790(91)90049-K","DOIUrl":null,"url":null,"abstract":"<div><p>Four closely related eclosion hormones (EHs), EH-I, -II, -III and -IV, were purified from 770,000 pharate adult heads of the silkworm, <em>Bombyx mori</em>. The complete amino acid sequence was determined by Edman degradation of peptide fragments generated by enzymatic digestion. Preliminary results have been reported (Kono <em>et al., Agric. biol. Chem.</em><strong>51</strong>, 2307–2308, 1987). Accumulated data suggested that EH-IV has the longest sequence consisting of 62 residues. EH-I and -III have N-termini truncated by two residues. EH-I and -II terminate at position 61. The removal of the C-terminal leucine in EH-I and -II might have occurred artificially during extraction.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 2","pages":"Pages 185-195"},"PeriodicalIF":0.0000,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90049-K","citationCount":"11","resultStr":"{\"title\":\"Isolation and complete amino acid sequences of eclosion hormones of the silkworm, Bombyx mori\",\"authors\":\"Takaharu Kono , Hiromichi Nagasawa , Akira Isogai , Hajime Fugo , Akinori Suzuki\",\"doi\":\"10.1016/0020-1790(91)90049-K\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Four closely related eclosion hormones (EHs), EH-I, -II, -III and -IV, were purified from 770,000 pharate adult heads of the silkworm, <em>Bombyx mori</em>. The complete amino acid sequence was determined by Edman degradation of peptide fragments generated by enzymatic digestion. Preliminary results have been reported (Kono <em>et al., Agric. biol. Chem.</em><strong>51</strong>, 2307–2308, 1987). Accumulated data suggested that EH-IV has the longest sequence consisting of 62 residues. EH-I and -III have N-termini truncated by two residues. EH-I and -II terminate at position 61. The removal of the C-terminal leucine in EH-I and -II might have occurred artificially during extraction.</p></div>\",\"PeriodicalId\":13955,\"journal\":{\"name\":\"Insect Biochemistry\",\"volume\":\"21 2\",\"pages\":\"Pages 185-195\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-1790(91)90049-K\",\"citationCount\":\"11\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Insect Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/002017909190049K\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Insect Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/002017909190049K","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 11
摘要
从77万份家蚕成虫头中分离得到4种密切相关的羽化激素,EH-I、-II、-III和-IV。完整的氨基酸序列是通过酶切产生的肽片段的Edman降解确定的。已经报告了初步结果(Kono et al., Agric。医学杂志。化学,51,2307-2308,1987)。累积数据表明EH-IV序列最长,包含62个残基。EH-I和-III的n端被两个残基截断。EH-I和-II终止于61号位置。EH-I和-II中c端亮氨酸的去除可能是在提取过程中人为发生的。
Isolation and complete amino acid sequences of eclosion hormones of the silkworm, Bombyx mori
Four closely related eclosion hormones (EHs), EH-I, -II, -III and -IV, were purified from 770,000 pharate adult heads of the silkworm, Bombyx mori. The complete amino acid sequence was determined by Edman degradation of peptide fragments generated by enzymatic digestion. Preliminary results have been reported (Kono et al., Agric. biol. Chem.51, 2307–2308, 1987). Accumulated data suggested that EH-IV has the longest sequence consisting of 62 residues. EH-I and -III have N-termini truncated by two residues. EH-I and -II terminate at position 61. The removal of the C-terminal leucine in EH-I and -II might have occurred artificially during extraction.