Please use this identifier to cite or link to this item:
http://hdl.handle.net/11455/36128
DC Field | Value | Language |
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dc.contributor | 王國祥 | zh_TW |
dc.contributor | 李龍湖 | zh_TW |
dc.contributor | 劉秉慧 | zh_TW |
dc.contributor.advisor | 王敏盈 | zh_TW |
dc.contributor.author | 何靜宜 | zh_TW |
dc.contributor.author | Ho, Jin-Yi | en_US |
dc.contributor.other | 中興大學 | zh_TW |
dc.date | 2007 | zh_TW |
dc.date.accessioned | 2014-06-06T07:53:55Z | - |
dc.date.available | 2014-06-06T07:53:55Z | - |
dc.identifier | U0005-2708200617432600 | zh_TW |
dc.identifier.citation | 林育江。2003。傳染性華氏囊病毒結構蛋白VP2之C端區域對形成次病毒顆粒及免疫力之影響。碩士論文。中興大學生物科技所。台中。 楊道翔。2005。利用昆蟲幼蟲生產傳染性華氏囊炎病毒結構蛋白VP2之次病毒顆粒及其應用。碩士論文。中興大學生物科技所。台中。 Azad, A. A., S. A. Barrett, and K. J. Fahey. 1985. The characterization and molecular cloning of the double-stranded RNA genome of an Australian strain of infectious bursal disease virus. Virology 143:35-44. Azad, A. A., M. N. Jagadish, M. A. Brown, and P. J. Hudson. 1987. Deletion mapping and expression in Escherichia coli of the large genomic segment of a birnavirus. Virology 161:145-52. Baumert, T. F., S. Ito, D. T. Wong, and T. J. Liang. 1998. Hepatitis C virus structural proteins assemble into viruslike particles in insect cells. J. Virol. 72:3827-36. Becht, H., H. M | zh_TW |
dc.identifier.uri | http://hdl.handle.net/11455/36128 | - |
dc.description.abstract | VP2蛋白是傳染性華氏囊病病毒的主要結構蛋白之ㄧ,亦是誘發宿主產生中和性抗體的免疫原。昆蟲細胞表現系統VP2蛋白(452H)會自我組裝形成T=1的次病毒顆粒。目前次病毒顆粒的結構已獲得2.6 | zh_TW |
dc.description.abstract | VP2 is the structure proteins of IBDV capsid and the primary host-protective immunogen of IBDV. When expressed in insect cell, VP2-452H spontaneously forms a T=1 subviral particle (SVP). Although the structure of SVP has been determined at 2.6 | en_US |
dc.description.tableofcontents | 圖次………………………………………………………………………4 表次…………………………………………………………………… 7 中文摘要…………………………………………………………………9 英文摘要...............................................10 第壹章、前言………………………………………………………….12 1. 家禽傳染性華氏囊病病毒之背景介紹…………………………12 2. 家禽傳染性華氏囊病病毒基因體組成及蛋白產物……………13 3. 病毒顆粒立體結構之研究………………………………………16 4. 以次病毒顆粒當作疫苗或載體…………………………………21 5. 研究動機及目的…………………………………………………23 第貳章、材料與方…………………………………………………….25 1. 細胞與病毒………………………………………………………25 2. 抗體的製備………………………………………………………28 3. 重組病毒之構築及製備…………………………………………28 4. 重組蛋白之表現…………………………………………………32 5. 重組蛋白之分析與鑑定…………………………………………33 6. 重組蛋白之純化…………………………………………………35 7. 穿透式電子顯微鏡觀察…………………………………………36 8. 雞隻之免疫試驗…………………………………………………37 9. 免疫試驗之分 析............... ..............38 10. 以次病毒顆粒抑制IBDV感染DF-1細胞…………………………40 第 | zh_TW |
dc.language.iso | en_US | zh_TW |
dc.publisher | 生物科技學研究所 | zh_TW |
dc.relation.uri | http://www.airitilibrary.com/Publication/alDetailedMesh1?DocID=U0005-2708200617432600 | en_US |
dc.subject | IBDV | en_US |
dc.subject | 傳染性華氏囊病毒 | zh_TW |
dc.subject | virus-like particle | en_US |
dc.subject | truncation | en_US |
dc.subject | IMAC | en_US |
dc.subject | 似病毒顆粒 | zh_TW |
dc.subject | 截切 | zh_TW |
dc.subject | 固定化金屬層析 | zh_TW |
dc.title | 傳染性華氏囊病毒的VP2蛋白 N端及C端序列對於T=1 次病毒顆粒的組裝與純化及免疫原性之影響 | zh_TW |
dc.title | Effect of terminal sequences of capsid protein VP2 of infectious bursal disease virus on the formation, purification and immunogenicity of T=1 subviral particles | en_US |
dc.type | Thesis and Dissertation | zh_TW |
item.openairetype | Thesis and Dissertation | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.languageiso639-1 | en_US | - |
item.grantfulltext | none | - |
item.fulltext | no fulltext | - |
item.cerifentitytype | Publications | - |
Appears in Collections: | 生物科技學研究所 |
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