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DC 欄位 | 值 | 語言 |
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dc.contributor.author | Pei-Ling Tsai | en |
dc.contributor.author | 蔡珮玲 | zh_TW |
dc.date.accessioned | 2021-07-01T08:12:47Z | - |
dc.date.available | 2021-07-01T08:12:47Z | - |
dc.date.issued | 2002 | |
dc.identifier.citation | Bjarnason, J.B. & Fox, J.W. (1995) Snake venom metalloendopeptidases: reprolysins. Methodes Enzymol. 248, 345-68.
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(1997) Spermine Inhibits Proinflammatory Cytokine Synthesis in Human Mononuclear Cells: A Counterregulatory Mechanism that Restrains the Immune Response. J. Exp. Med. 185, 1759-68. 詹靜怡 (1997)鯉魚腎泌分解?作用於頭腎細胞間質之生化證據,國立臺灣大學動物學研究所碩士論文。 郭弘億 (1998)鯉魚腎泌分解?酵素活性之調控,國立臺灣大學生化科學研究所碩士論文。 陳築瑄(1999)鯉魚腎泌分解?之內生性抑制蛋白之純化,國立臺灣大學生化科學研究所碩士論文。 | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75350 | - |
dc.description.abstract | 腎泌分解?是我們實驗室自鯉魚頭腎萃取液純化到的分泌性金屬耦合蛋白?,分子量約為23kD。其一級結構屬於astacin家族。腎泌分解?可與細胞間質中的肝制凝素(Heparin)等黏多醣類結合而滯留其中。主要分佈於鯉魚的頭腎、腎臟、及脾臟組織,是此家族成員中於淋巴造血器官中被發現的首例。之後我們利用肝制凝素親合力管柱在鯉魚腎臟純化到具有活性的腎泌分解?抑制蛋白,其分子量為40kDa且帶有醣類。在本篇論文裡,我們由蛋白質及其部分勝?片段的N端胺基酸序列設計聚合?連鎖反應的引子,進行抑制蛋白的基因選殖。得到兩種不同長度的cDNA株,其中序列較長的cDNA株,在3’端的附近包含一段特殊的重覆序列。兩者的轉譯蛋白質都包含signal peptide,顯示出此蛋白質屬於分泌性蛋白。轉譯的序列經比對後發現其一級結構和哺乳動物的胎兒蛋白家族相似。胎兒蛋白主要表現在胚胎的血液、肝臟、腦脊髓液和大腦中,參與組織的分化和轉型,尤其在神經系統發育和免疫反應的調控中扮演重要的角色。此外,我們還發現腎泌分解?抑制蛋白在初始合成是一個65kDa的前驅分子,分泌到細胞外後透過血液分佈到其他組織。當它進入淋巴造血器官時,會被蛋白?切割成40kDa的分子而成為具有抑制活性的蛋白質。 Fetuin 的 processing 現象,迄今尚未被報導過,在此我們所發表的腎泌分解?內生性抑制蛋白,是astacin蛋白?家族中第一個被發現的抑制蛋白,相信astacin家族中的其他成員亦可能有內生性抑制蛋白存在,負責調節其活性與功能。 | zh_TW |
dc.description.abstract | Nephrosin is a newly discovered member of the astacin family. It is a secreted proteinase and present in the head kidney, kidney, and spleen, all of which are responsible for the immune and haematopoietic function in fish. We have recently purified the nephrosin inhibitor from carp kidney extract by heparin affinity chromatography. Its inhibitory activity has also been confirmed by reverse zymography. In this study, we have cloned the cDNA encoding for the nephrosin inhibitor. There are two different cDNA clones resulting from alternative splicing, and the long form contains unique tandem repeat sequences in the 3’end. Both of them have signal peptides suggesting that they are a secreted protein. The deduced primary structure of nephrosin inhibitor is similar to fetuin-A, a mammalian fetal protein present in fetal blood, liver, cerebrospinal fluid, and cerebral cortex during the fetal development. Although its real physiological function remains elusive, it is involved in tissue differentiation and transformation, especially in the nervous and immune systems. We also found that the nephrosin inhibitor was synthesized initially as a precursor in liver and then secreted to the blood. When it was distributed into the hematopoietic tissues, it could be processed from molecular weight 65kDa to 40kDa and acquired inhibitory activity. This processing phenomenon of fetuin has not been reported elsewhere. More importantly the presence of an endogenous inhibitor of nephrosin is the first report of this kind in astacin enzymes. It is very likely that endogenous inhibitors may also be present for the regulation of other astacin enzymes. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:12:47Z (GMT). No. of bitstreams: 0 Previous issue date: 2002 | en |
dc.description.tableofcontents | 目錄 …………………………………………………………………………………………………………………………I 中文摘要 ……………………………………………………………………………………………………………………Ⅲ 英文摘要 ……………………………………………………………………………………………………………………Ⅳ 第一章 前言 第一節 腎泌分解?……………………………………………………………………………………………………1 第二節 Astacin 家族…………………………………………………………………………………………………2 第三節 尋找腎泌分解?內生性抑制蛋白……………………………………………………………………………2 第四節 胎兒蛋白(Fetuin)……………………………………………………………………………………………3 第五節 胎兒蛋白的功能………………………………………………………………………………………………5 第二章 材料與實驗方法 第一節 實驗動物………………………………………………………………………………………………………8 第二節 SDS聚丙烯醯胺凝膠電泳(SDS-PAGE)………………………………………………………………………8 第三節 蛋白質膠片染色………………………………………………………………………………………………9 第四節 西方轉印法(Western blotting)……………………………………………………………………………9 第五節 鯉魚組織萃取液的製備………………………………………………………………………………………10 第六節 蛋白質N 端定序………………………………………………………………………………………………10 第七節 雙硫鍵的還原和修飾…………………………………………………………………………………………11 第八節 抑制蛋白之醣類移除及質譜分析……………………………………………………………………………11 第九節 自鯉魚血清中純化腎泌分解?內生性抑制蛋白之前驅……………………………………………………12 第十節 Processing assay……………………………………………………………………………………………13 第十一節 Reverse zymography…………………………………………………………………………………………14 第十二節 腎泌分解?和抑制蛋白複合體的純化………………………………………………………………………15 第十三節 以肝制凝素管柱除去複合體…………………………………………………………………………………15 第十四節 鯉魚組織全部核醣核酸的製備(total RNA)………………………………………………………………16 第十五節 純化mRNA………………………………………………………………………………………………………16 第十六節 製備第一股去氧核醣核酸……………………………………………………………………………………17 第十七節 degenerate primers的合成…………………………………………………………………………………17 第十八節 聚合?連鎖反應………………………………………………………………………………………………18 第十九節 洋菜膠電泳……………………………………………………………………………………………………18 第二十節 Agarose Gel Elution………………………………………………………………………………………19 第二十一節 核酸的接合與轉化作用……………………………………………………………………………………19 第二十二節 質體 DNA的製備……………………………………………………………………………………………20 第二十三節 Rapid Applification of cDNA Ends……………………………………………………………………20 第二十四節 北方轉印法(Northern Blotting)………………………………………………………………………21 第三章 實驗結果 第一節 腎泌分解?抑制蛋白之N端序列分析及聚合?連鎖反應之引子合成………………………………………24 第二節 腎泌分解?抑制蛋白之 cDNA選殖及定序……………………………………………………………………25 第三節 腎泌分解?抑制蛋白和哺乳動物胎兒蛋白基因(fetuin)間的相似度……………………………………26 第四節 腎泌分解?抑制蛋白 mRNA的組織分佈………………………………………………………………………27 第五節 抑制蛋白以40kDa(Processed form)的型式存在腎泌分解?大量表現的組織中…………………………27 第六節 腎泌分解?抑制蛋白(65kDa)的活性測試……………………………………………………………………28 第七節 大部分40kDa的抑制蛋白會和腎泌分解?形成複合體而非以自由型式存在免疫造血組織中……………29 第四章 討論 第一節 腎泌分解?抑制蛋白是胎兒蛋白家族的成員 ………………………………………………………………30 第二節 腎泌分解?抑制蛋白的組織分佈與存在型式 ………………………………………………………………32 第三節 腎泌分解?抑制蛋白的活性測試 ……………………………………………………………………………33 結語與未來研究方向 ………………………………………………………………………………………………………35 參考資料 ……………………………………………………………………………………………………………………36 圖表 …………………………………………………………………………………………………………………………43 | |
dc.language.iso | zh-TW | |
dc.title | 鯉魚腎泌分解?內生性抑制蛋白之基因選殖及鑑定 | zh_TW |
dc.title | Cloning and Identification of an Endogenous Nephrosin Inhibitor from Carp | en |
dc.date.schoolyear | 90-2 | |
dc.description.degree | 碩士 | |
dc.relation.page | 64 | |
dc.rights.note | 未授權 | |
dc.contributor.author-dept | 生命科學院 | zh_TW |
dc.contributor.author-dept | 生化科學研究所 | zh_TW |
顯示於系所單位: | 生化科學研究所 |
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