{"title":"家蚕血淋巴幼体激素结合蛋白的纯化及特性研究","authors":"Keiji Kurata , Masatoshi Nakamura , Takashi Okuda , Hisashi Hirano , Hiroshi Shinbo","doi":"10.1016/0305-0491(94)90147-3","DOIUrl":null,"url":null,"abstract":"<div><p>A juvenile hormone binding protein (JHBP) has been isolated from <em>Bombyx mori</em> hemolymph by gel filtration, ion-exchange chromatography, chromatofocusing and hydroxyapatite column chromatography. Gel electrophoresis indicates that the isolated protein is homogeneous in the presence or absence of a denaturing agent. The JHBP in question has a relative molecular mass of 32 kDa, determined by denaturing gel electrophoresis. Chromatofocusing analysis indicated that the JHBP is an acidic protein with pI 4.9. The protein exhibits a dissociation constant of 9.0 × 10<sup>−8</sup> M for JH I, 1.14 × 10<sup>−7</sup> M for JH II and 3.9 × 10<sup>−7</sup> M for JH III, and thus its affinity for JH analogues is in the order of <em>JH</em><em>I</em> ><em>JH</em><em>II</em> ><em>JH</em><em>III</em>. Its amino acid composition indicates that the protein consists of 297 residues of 18 kinds of amino acids. The sequence of the N-terminus of the polypeptide chain was determined for 34 of the first 36 residues: Asp-Gln-Asp-Ala-Leu-Leu-Lys-Pro-?-Lys-Leu-Gly-Asp-Met-Gln-Ser-Leu-Ser-Ser-Ala-Thr-Gln-Gln-Phe-Leu-Glu- Lys-Thr-Ser-Lys-Gly-Ile-Pro-?-Tyr-His-.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 105-114"},"PeriodicalIF":0.0000,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90147-3","citationCount":"18","resultStr":"{\"title\":\"Purification and characterization of a juvenile hormone binding protein from hemolymph of the silkworm, Bombyx mori\",\"authors\":\"Keiji Kurata , Masatoshi Nakamura , Takashi Okuda , Hisashi Hirano , Hiroshi Shinbo\",\"doi\":\"10.1016/0305-0491(94)90147-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>A juvenile hormone binding protein (JHBP) has been isolated from <em>Bombyx mori</em> hemolymph by gel filtration, ion-exchange chromatography, chromatofocusing and hydroxyapatite column chromatography. Gel electrophoresis indicates that the isolated protein is homogeneous in the presence or absence of a denaturing agent. The JHBP in question has a relative molecular mass of 32 kDa, determined by denaturing gel electrophoresis. Chromatofocusing analysis indicated that the JHBP is an acidic protein with pI 4.9. The protein exhibits a dissociation constant of 9.0 × 10<sup>−8</sup> M for JH I, 1.14 × 10<sup>−7</sup> M for JH II and 3.9 × 10<sup>−7</sup> M for JH III, and thus its affinity for JH analogues is in the order of <em>JH</em><em>I</em> ><em>JH</em><em>II</em> ><em>JH</em><em>III</em>. Its amino acid composition indicates that the protein consists of 297 residues of 18 kinds of amino acids. The sequence of the N-terminus of the polypeptide chain was determined for 34 of the first 36 residues: Asp-Gln-Asp-Ala-Leu-Leu-Lys-Pro-?-Lys-Leu-Gly-Asp-Met-Gln-Ser-Leu-Ser-Ser-Ala-Thr-Gln-Gln-Phe-Leu-Glu- Lys-Thr-Ser-Lys-Gly-Ile-Pro-?-Tyr-His-.</p></div>\",\"PeriodicalId\":100294,\"journal\":{\"name\":\"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry\",\"volume\":\"109 1\",\"pages\":\"Pages 105-114\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0305-0491(94)90147-3\",\"citationCount\":\"18\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0305049194901473\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0305049194901473","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Purification and characterization of a juvenile hormone binding protein from hemolymph of the silkworm, Bombyx mori
A juvenile hormone binding protein (JHBP) has been isolated from Bombyx mori hemolymph by gel filtration, ion-exchange chromatography, chromatofocusing and hydroxyapatite column chromatography. Gel electrophoresis indicates that the isolated protein is homogeneous in the presence or absence of a denaturing agent. The JHBP in question has a relative molecular mass of 32 kDa, determined by denaturing gel electrophoresis. Chromatofocusing analysis indicated that the JHBP is an acidic protein with pI 4.9. The protein exhibits a dissociation constant of 9.0 × 10−8 M for JH I, 1.14 × 10−7 M for JH II and 3.9 × 10−7 M for JH III, and thus its affinity for JH analogues is in the order of JHI >JHII >JHIII. Its amino acid composition indicates that the protein consists of 297 residues of 18 kinds of amino acids. The sequence of the N-terminus of the polypeptide chain was determined for 34 of the first 36 residues: Asp-Gln-Asp-Ala-Leu-Leu-Lys-Pro-?-Lys-Leu-Gly-Asp-Met-Gln-Ser-Leu-Ser-Ser-Ala-Thr-Gln-Gln-Phe-Leu-Glu- Lys-Thr-Ser-Lys-Gly-Ile-Pro-?-Tyr-His-.
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