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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/10029完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 蔡蔭和(Inn-Ho Tsai) | |
| dc.contributor.author | Xin-hong Yu | en |
| dc.contributor.author | 余信宏 | zh_TW |
| dc.date.accessioned | 2021-05-20T20:56:51Z | - |
| dc.date.available | 2016-08-02 | |
| dc.date.available | 2021-05-20T20:56:51Z | - |
| dc.date.copyright | 2011-08-02 | |
| dc.date.issued | 2011 | |
| dc.date.submitted | 2011-07-28 | |
| dc.identifier.citation | 1. Toshiaki N., Yumik K. Kinin-releasing and kinin-degrading enzyme, in: Enzymes from snake venom. Bailey G. S. (Ed), Alaken, Colorado, 1998; pp.287-316
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Comparative characterisation of Russell's viper (Daboia/Vipera russelii) venoms from different regions of the Indian peninsula. Biochim Biophys Acta. 1999;1428:121-36. 56. Meier J, Freyvogel TA. Comparative studies on venoms of the fer-de-lance (Bothrops atrox), carpet viper (Echis carinatus) and spitting cobra (Naja nigricollis) snakes at different ages. Toxicon. 1980;18:661-2. 57. Furtado MF, Maruyama M, Kamiguti AS, Antonio LC. Comparative study of nine Bothrops snake venoms from adult female snakes and their offspring. Toxicon. 1991;29:219-26. 58. Siigur E, Aaspõllu A, Tu AT, Siigur J. cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom. Biochem Biophys Res Commun. 1996;224:229-36. 59. Siigur E, Siigur J. Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom. Biochim Biophys Acta. 1991;1074:223-9. 60. Siigur E, Tõnismägi K, Trummal K, Samel M, Vija H, Aaspõllu A, Rönnholm G, Subbi J, Kalkkinen N, Siigur J. A new tyrosine-specific chymotrypsin-like and angiotensin-degrading serine proteinase from Vipera lebetina snake venom. Biochimie. 2011;93:321-30. 61. Yamada D, Sekiya F, Morita T. Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism. J Biol Chem. 1996;271:5200-7. 62. Tsai IH, Wang YM, Cheng AC, Starkov V, Osipov A, Nikitin I, Makarova Y, Ziganshin R, Utkin Y. cDNA cloning, structural, and functional analyses of venom phospholipases A_2 and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii renardi. Toxicon. 2011;57:332-41. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/10029 | - |
| dc.description.abstract | 本篇研究目的在於發現並了解Vipera ursinii renardi蛇毒內的促凝蛋白，Vipera ursinii renardi的蛇毒先前較少被研究，因此仍然存在著許多未知。利用前人已發表的類似蛋白的cDNA序列可設計出特殊的primer，並可經由PCR放大所需的基因，在本研究中已利用此技術成功放大了Vipera ursinii renardi蛇囊內編碼Factor X activator subunits與Factor V activator的基因，其中在絲胺酸蛋白酶的部分，除了FV activator (本文稱之為Vur-FVA)還發現了chymotrypsin-like protease，前者的氨基酸序列與Vipera lebetina FV activator的具有93%的高度相似性，而後者與V. lebetina的chymotrypsin-like protease也具有90%的相似性，Vur-FVA可經由凝膠層析(gel filtration)與陽離子交換(cation exchanger )管柱而被純化出來，並可經由SDS-PAGE觀察到Vur-FVA具有將FV活化的能力。除了Vipera ursinii renardi 蛇毒活化FX的能力外，本研究中亦測量了其他許多Vipernae的蛇毒，儘管V. u. renard蛇毒活化FX的能力比Russell`s viper弱了上百倍，然而其蛇毒確實具有FX activator的活性，V. u. renardi FX activator在本研究中被命名為Vur-FXA，經過凝膠層析(gel filtration)管柱的初步純化後我們觀察到Vur-FXA的分子量大概為95 kDa，且經由SDS-PAGE 的分析可得知Vur-FXA具有多個subunit。研究中還經由基因選殖的技術，發現了Vur-FXA的CTLL light chains與Vipera lebetina 和Daboia russelli的CTLL light chains具有高度的相似性，而針對Vur-FXA heavy chain的部分，我們得到了一個pIII金屬蛋白酶，然而卻發現其缺少了負責與light chains形成雙硫鍵的Cysteine。由以上結果可發現V. u. renardi蛇毒中具有多種促凝成份，這些成份可能會與前人在V. u. renardi蛇毒中所發現的抗凝成份具有協同作用，共同造成凝血症狀或獵物的死亡，因此未來可針對此一現象做更深入的研究。 | zh_TW |
| dc.description.abstract | The aim of this study is to identify and characterize the pro-coagulant proteins in the venom of a less studied Viperinae species, Vipera ursinii renardi. Using the specific primers designed based on previously published cDNA sequences of the pro-coagulant proteases from the other two Viperinae species, we have cloned the cDNA encoding all the subunits or proteins of Factor X and Factor V activators from the venom glands of V. u. renardi (Vur). Two distinct serine proteases have been cloned from Vur cDNAs. One encodes a FV activator, and the other encodes a chymotrypsin-like protease. The deduced amino acid sequence of the former enzyme revealed 93% identity with Vipera lebetina FV activator and was designated as Vur-FVA. Another was 90% identical to a chymotrypsin-like protease of V. lebetina. Vur-FVA was purified from the crude venom by gel filtration and cation exchanger columns; its FV activating activity was confirmed by SDS-PAGE analysis of the produced FVa. FX activating activities of many Vipernae venoms were compared by assay the FXa generated. Although the activity is 2 order of magnitude weaker than Russell`s viper venom, V. u. renardi venom do contain the activity. The FX activator (designated as Vur-FXA) was partially purified by gel filtration and shown the molecular weight is about 95 kDa. We also could find Vur-FXA was a oligomer by comparing the fractions containing Vur-FXA on reducing and non-reducing SDS-PAGE gel. The CTLL light chains of Vur-FXA were cloned and the deduced amino acid sequences are highly similar to those of V. lebetina and Daboia russelli. The amino acid sequence of a PIII metalloprotease was also cloned. However, the deduced protease sequence lacks the Cys residue which involved in disulfide linking to the light chain in RVV-X. These results characterized Vur venom pro-coagulant components. It has been reported anticoagulant components exist in Vur venom. The anticoagulant components and procoagulant components may act synergistically, leading to coagulopathy symptom or the death of prey. | en |
| dc.description.provenance | Made available in DSpace on 2021-05-20T20:56:51Z (GMT). No. of bitstreams: 1 ntu-100-R98b46017-1.pdf: 2917438 bytes, checksum: b5abdc71d8d6b8e468e71451c40c69f4 (MD5) Previous issue date: 2011 | en |
| dc.description.tableofcontents | 中文摘要 (I)
Aabstrate (II) Lists of abbreviations (IV) Lists of Figures (V) Lists of Table (VI) 1.Introduction (1) 2. Materials and methods (13) 2-1. Venoms and other materials (13) 2-2. Cloning and sequencing (13) 2-3. Protein quantification (15) 2-4. SDS- polyacrylamide gel electrophoresis (15) 2-5. Purification of Vur-FVA (15) 2-6. Peptide mass fingerprinting (16) 2-7. N-terminal sequencing (16) 2-8. Hydrolysis of human coagulation factor V by Vur-FVA (17) 2-9. Phylogenetic analysis of CTL and CTLLs (17) 2-10. Chromogenic assay of venom factor X activator activity (17) 2-11. Purification of Vur-FXA (18) 3. Results (19) 3-1. cDNA cloning and the predicted sequence of Vur-FVA (19) 3-2. Sequence alignment and comparison between related venom serine proteases (20) 3-3. Purification and characterization of Vur-FVA (20) 3-4. Proteolytic activity of Vur-FVA toward human coagulation factor V (20) 3-5. cDNA cloning and the predicted sequence of C-typr lectin and C-type lectin (21) 3-6. Chromogenic assay of crude venom factor X activator activity (21) 3-7. cDNA cloning and the predicted sequence of Vur-FXA (22) 3-8. Sequence alignment and comparison between the published snake venom FX activator heavy chains (22) 3-9. Purification and characterization of Vur-FXA (23) 4. Discussion (41) 5. Reference (45) 6. Appendix (53) | |
| dc.language.iso | zh-TW | |
| dc.title | 草原蝰(Vipera ursinii renardi)蛇毒促凝蛋白酶的基因選殖
與特性 | zh_TW |
| dc.title | cDNA cloning and protein characterization of the
pro-coagulant proteases from Vipera ursinii renardi venom | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 99-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 朱善德(Sin-Tak Chu),李明亭(Ming-Ting Lee),林淑華(Shu-Wha Lin) | |
| dc.subject.keyword | 草原蝰,促凝蛋白酶, | zh_TW |
| dc.subject.keyword | Vipera ursinii renardi,pro-coagulant proteases, | en |
| dc.relation.page | 53 | |
| dc.rights.note | 同意授權(全球公開) | |
| dc.date.accepted | 2011-07-28 | |
| 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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