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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 陳義雄(Yee-Hsiung Chen) | |
dc.contributor.author | Huan-Chin Tseng | en |
dc.contributor.author | 曾煥清 | zh_TW |
dc.date.accessioned | 2021-06-15T03:02:13Z | - |
dc.date.available | 2009-08-06 | |
dc.date.copyright | 2009-08-06 | |
dc.date.issued | 2009 | |
dc.date.submitted | 2009-07-30 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/44513 | - |
dc.description.abstract | 小鼠貯精囊分泌液以還原性 SDS-PAGE 電泳分析,可以觀察到七個明顯的蛋白,按照分子量大小命名為 SVS I-VII。而實際上在貯精囊液中幾乎沒有 SVS I、SVS II、和SVS III以單體形式存在,它們會以雙硫鍵連結成分子量非常大的不同蛋白質複合體 (high molecular weight complexes, HMWCs)。經由免疫組織染色法證明 SVS I、SVS II、SVS III蛋白是組成交配栓的蛋白成分。將交配栓以還原性SDS-PAGE sample buffer 粹取,幾乎沒有 SVS I 和 SVS II 被溶解出來,只有少量 SVS III 會被溶解出來,顯示在交配栓中 SVS I-III 之間除了雙硫鍵之外還有其他共價鍵參與其中。進一步純化凝固腺中轉麩胺醯酶 (TG4),並且與組織內的轉麩胺醯酶 (TG2) ,比較催化貯精囊分泌蛋白的酵素活性。我們發現 TG4 對於 HMWCs 具有較高的活性。然而 TG2 對於還原後貯精囊液中自由的 SVS I-III 蛋白具有較佳的活性。這種高效率的 TG4 催化在,精液凝固而形成交配栓是一重要的生化反應,其生殖的意義會加以討論。
SVS I 蛋白質序列共有 820 個胺基酸,其中 43 個為麩胺酸 43 個為離胺酸。,我們根據其序列製備 7 段重組蛋白,分成 1-78 胺基酸序列為 F1 片段、79-259 胺基酸序列為 F2 片段、260-405 胺基酸序列為 F3 片段、406-500 胺基酸序列為 F4 片段、501-650 胺基酸序列為 F5 片段、651-715 胺基酸序列為 F6 片段以及 716-796 胺基酸序列為 F7 片段。比較 F1~F7 片段被 TG4 催化後所接上 BPNH2 或 A25 peptide的數量。F2 片段對於 BPNH2 作用的活性遠大於其他片段,而 A25 peptide 對於各片段的反應活性相對較低。質譜分析經 TG4 催化,而連結上 BPNH2 的 F2 片段,鑑定出 Q232 和 Q254 是TG4 作用標的。將 F2 片段的 Q232 和 Q254 突變為三種 F2 片段 (Q232G、Q254G 和Q232G/Q254G),BPNH2 連接上去的數量相對原始 F2 片段減少,確認 Q232 和 Q254 為 TG4 催化的主要目標。 | zh_TW |
dc.description.abstract | Resolution of mouse seminal vesicle secretion (SVS) by reducing SDS-PAGE can clearly identified seven major monomer proteins tentatively designated as SVS I-VII according to the decreasing order of their molecular masses. However, no monomer forms of SVS I-III are present in SVS. Instead, they appear in various high molecular weight complexes (HMWCs) formed by inter-polypeptide disulfide bridges among SVS I, SVS II and SVS III. The HMWCs become the predominant protein in SVS. We were able to immunodetect SVS I-III in cross sections of mouse copulatory plug. Heating the clotted lump in SDS-PAGE sample buffer in the presence of DTT released none of SVS I or SVS II but only a trace of SVS III into the solution, indicative of covalent cross-links in addition to disulfide bonds among the SVS I-III proteins in the plug. Further, we purified type 4 transglutaminase (TG4) from the mouse coagulating gland to homogeneity, and compared it to type 2 transglutaminase (TG2) from guinea pig liver in terms of enzymatic ability to cross-link proteins in the SVS. We found that TG4 showed much greater activity than TG2 in catalyzing the cross-links between HMWC proteins. On the contrary, it was less active than TG2 in cross-linking any of the free SVS I-III proteins released from the reduced HMWC. The reproductive significance of more efficient TG4 catalysis is discussed.
Based on the SVSI-deduced protein sequence, SVS I contains 820 amino acid residues in which there are 43 glutamine and 43 lysine residues. We produced 7 recombinant polypeptide fragments including residues 1-78/F1, residues 79-259/F2, residues 260-405/F3, residues 406-500/F4, residues 501-650/F5, residues 651-715/F6, and residues 716-796/F7, and measured the covalent incorporation of 5-(biotinamido)pentylamine (BPNH2) or biotin-TVQQEL (A25 peptide) to each of F1-to-F7 by TG4. F2 was much more active than the other fragments during the BPNH2-glutamine incorporation, Relatively, a low extent of A25 cross-linking to any one of the seven polypeptide fragments was observed. The MS analysis of BPNH2-F2 conjugate identified Q232 and Q254 as the two major TG4 cross-linking sites. This was substantiated by the result that much less BPNH2 was cross-linked to any one of three F2 mutants, including Q232G and Q254G obtained from single-site mutation, and Q232G/Q254G from double-site mutation. | en |
dc.description.provenance | Made available in DSpace on 2021-06-15T03:02:13Z (GMT). No. of bitstreams: 1 ntu-98-D92b46012-1.pdf: 1901718 bytes, checksum: 6f51ce62ec8f1fcd001e33a420bb97e6 (MD5) Previous issue date: 2009 | en |
dc.description.tableofcontents | 縮寫表 III
摘要 IV Abstract V 第一章 緒論 1 1.1 生殖學概論 1 1.2 哺乳類雄性生殖系統 1 1.3 附屬性腺的研究 2 1.3.1 附屬性腺的差異 2 1.3.2 附屬性腺的生理功能 3 1.3.3 附屬性腺的病理研究 4 1.4 前列腺的發育與功能 4 1.5 貯精囊發育與功能 4 1.6 交配栓 6 1.6.1 交配栓的形成 6 1.6.2 交配栓的功能 6 1.7 轉麩胺醯胺酶的功能 7 1.7.1 轉麩胺醯胺酶的分類 7 1.7.2 轉麩胺醯胺酶催化的轉化醯基反應 8 1.7.3 轉麩胺醯胺酶的活性反應區和結構 8 1.7.4轉麩胺醯胺酶的基質選擇性 9 1.8 研究背景 10 1.8.1小白鼠貯精囊 SVS I 之研究 10 1.8.2交配栓內貯精囊液蛋白的共價鍵結 11 第二章 材料與方法 12 2.1實驗材料 12 2.1.1 化學試劑與酵素 12 2.1.2 實驗動物 12 2.2 SVS I-III 抗體製備 12 2.2.1 重組質體的製備 12 2.2.2 重組蛋白的純化 13 2.3 免疫組織染色 13 2.4 對角線電泳分析 14 2.5 小鼠 TG4 純化 14 2.6 Solid-Phase Microtiter Assay 15 2.7 蛋白質交聯實驗 15 2.8 SVS I F1-F7 片段的製備 15 2.8.1 重組質體的製備 15 2.8.2 重組蛋白的純化 16 2.9 製備接上 BPNH2 的 SVS I F2 片段 17 第三章 實驗結果 18 3.1交配栓內貯精囊液蛋白的共價鍵結 18 3.1.1小鼠 SVS I、SVS II、SVS III 抗體製備 18 3.1.2 SVS I-III是交配栓的組成成分 18 3.1.3 貯精囊分泌蛋白 SVS I-III 會形成高分子聚合物 18 3.1.4交配栓內 SVS I-III 之間共價鍵結 19 3.1.5 生殖系統特有的轉麩胺醯酶 19 3.1.6 純化及鑑定小鼠凝固腺分泌蛋白TG4 20 3.1.7 TG4酵素活性測定 20 3.1.8 在貯精囊分泌蛋白中SVS I-III是TG4的基質 21 3.1.9 HMWCs 分子間雙硫鍵對於TG作用的影響 21 3.2 鑑定貯精囊蛋白SVS I被凝固腺液之轉麩胺醯酶催化的活性部位 22 3.2.1 製備SVS I F1~F7片段重組蛋白 22 3.2.2 鑑定 SVS I 被催化的活性部位 22 第四章 討論 58 4.1 SVS I-III 參與交配栓的形成 58 4.2 TG4 催化 HMWCs 內的蛋白鍵結 58 4.3 小鼠 SVS I 與 TG 的作用 59 References 60 | |
dc.language.iso | zh-TW | |
dc.title | 探討交配栓內蛋白的共價鍵結
貯精囊蛋白SVS I被凝固腺液之轉麩胺醯酶催化的活性部位 | zh_TW |
dc.title | Study of Protein Cross-Links in Copulatory Plug
The Major TG4 Cross-linking Sites of SVS I in mouse Seminal Vesicle | en |
dc.type | Thesis | |
dc.date.schoolyear | 97-2 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 余榮熾(Lung-Chih Yu),李明亭(Ming-Ting Lee),梁博煌(Po-Huang Liang),蔡懷楨(Huai-Jen Tsai),黃彥華(Yen-Hua Huang),潘榮隆(Rong-Long Pan) | |
dc.subject.keyword | 貯精囊,凝固腺,轉麩胺醯酶,蛋白質交聯,精液凝結,交配栓, | zh_TW |
dc.subject.keyword | seminal vesicle,coagulating gland,transglutaminase,protein cross link,seminal coagulation,copulatory plug, | en |
dc.relation.page | 65 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2009-07-30 | |
dc.contributor.author-college | 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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