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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 莊榮輝 | |
| dc.contributor.author | Yan-Hung Chen | en |
| dc.contributor.author | 陳彥宏 | zh_TW |
| dc.date.accessioned | 2021-06-16T02:26:04Z | - |
| dc.date.available | 2018-08-16 | |
| dc.date.copyright | 2015-08-16 | |
| dc.date.issued | 2015 | |
| dc.date.submitted | 2015-08-05 | |
| dc.identifier.citation | Assche, F.V., and Clijsters, H. (1990). Effects of metals on enzyme activity in plants. Plant, Cell & Environment 13, 195-206.
Bernhard, W.R., and Kägi, J.H. (1987). Purification and characterization of atypical cadmium-binding polypeptides from Zea mays. In Metallothionein II (Springer), pp. 309-315. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry 72, 248-254. Cazalé, A.-C., and Clemens, S. (2001). Arabidopsis thaliana expresses a second functional phytochelatin synthase. Febs Letters 507, 215-219. Clemens, E.S., and Cook, J.M. (1999). Politics and institutionalism: Explaining durability and change. Annual review of sociology, 441-466. Clemens, S., Schroeder, J.I., and Degenkolb, T. (2001). Caenorhabditis elegans expresses a functional phytochelatin synthase. European Journal of Biochemistry 268, 3640-3643. Cobbett, C., and Goldsbrough, P. (2002). Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis. Annual review of plant biology 53, 159-182. Cobbett, C.S. (1999). A family of phytochelatin synthase genes from plant, fungal and animal species. Trends in plant science 4, 335-337. Cobbett, C.S. (2000). Phytochelatin biosynthesis and function in heavy-metal detoxification. Current opinion in plant biology 3, 211-216. Cruz, B.H., Dı́az-Cruz, J.M., Šestáková, I., Velek, J., Ariño, C., and Esteban, M. (2002). Differential pulse voltammetric study of the complexation of Cd (II) by the phytochelatin (γ-Glu Cys) 2 Gly assisted by multivariate curve resolution. Journal of Electroanalytical Chemistry 520, 111-118. Dietz, K.-J., Baier, M., and Krämer, U. (1999). Free radicals and reactive oxygen species as mediators of heavy metal toxicity in plants. In Heavy metal stress in plants (Springer), pp. 73-97. Dong, R., Formentin, E., Losseso, C., Carimi, F., Benedetti, P., Terzi, M., and Schiavo, F.L. (2005). Molecular cloning and characterization of a phytochelatin synthase gene, PvPCS1, from Pteris vittata L. Journal of Industrial Microbiology and Biotechnology 32, 527-533. Duffus, J.H. (2002). ' Heavy metals' a meaningless term?(IUPAC Technical Report). Pure and Applied Chemistry 74, 793-807. Eapen, S., and D'souza, S. (2005). Prospects of genetic engineering of plants for phytoremediation of toxic metals. Biotechnology advances 23, 97-114. Grill, E., Winnacker, E.-L., and Zenk, M.H. (1985). Phytochelatins: the principal heavy-metal complexing peptides of higher plants. Science 230, 674-676. Grill, E., Winnacker, E.-L., and Zenk, M. (1986). Synthesis of seven different homologous phytochelatins in metal-exposed Schizosaccharomyces pombe cells. FEBS letters 197, 115-120. Grill, E., Löffler, S., Winnacker, E.-L., and Zenk, M.H. (1989). Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase). Proceedings of the National Academy of Sciences 86, 6838-6842. Guo, J., Dai, X., Xu, W., and Ma, M. (2008). Overexpressing GSH1 and AsPCS1 simultaneously increases the tolerance and accumulation of cadmium and arsenic in Arabidopsisthaliana. Chemosphere 72, 1020-1026. Ha, S.-B., Smith, A.P., Howden, R., Dietrich, W.M., Bugg, S., O'Connell, M.J., Goldsbrough, P.B., and Cobbett, C.S. (1999). Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe. The Plant Cell Online 11, 1153-1163. He, Z., Li, J., Zhang, H., and Ma, M. (2005). Different effects of calcium and lanthanum on the expression of phytochelatin synthase gene and cadmium absorption in Lactuca sativa. Plant Science 168, 309-318. Herbette, S., Taconnat, L., Hugouvieux, V., Piette, L., Magniette, M.-L., Cuine, S., Auroy, P., Richaud, P., Forestier, C., and Bourguignon, J. (2006). Genome-wide transcriptome profiling of the early cadmium response of Arabidopsis roots and shoots. Biochimie 88, 1751-1765. Howden, R., Goldsbrough, P.B., Andersen, C.R., and Cobbett, C.S. (1995). Cadmium-sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient. Plant Physiology 107, 1059-1066. Küpper, H., Parameswaran, A., Leitenmaier, B., Trtílek, M., and Šetlík, I. (2007). Cadmium‐induced inhibition of photosynthesis and long‐term acclimation to cadmium stress in the hyperaccumulator Thlaspi caerulescens. New Phytologist 175, 655-674. Kirkby, M.a. (1987). Principles of plant nutrition. Internation Potash Institute, Beren-Worblaufen. Kobayashi, R., and Yoshimura, E. (2006). Differences in the binding modes of phytochelatin to Cadmium (II) and Zinc (II) ions. Biological trace element research 114, 313-318. Le Faucheur, S., Behra, R., and Sigg, L. (2005). Phytochelatin induction, cadmium accumulation, and algal sensitivity to free cadmium ion in Scenedesmus vacuolatus. Environmental toxicology and chemistry 24, 1731-1737. Lee, S., Moon, J.S., Ko, T.-S., Petros, D., Goldsbrough, P.B., and Korban, S.S. (2003). Overexpression of Arabidopsis phytochelatin synthase paradoxically leads to hypersensitivity to cadmium stress. Plant Physiology 131, 656-663. Li, J., Guo, J., Xu, W., and Ma, M. (2006). Enhanced cadmium accumulation in transgenic tobacco expressing the phytochelatin synthase gene of Cynodon dactylon L. Journal of Integrative Plant Biology 48, 928-937. Li, Y., Dhankher, O.P., Carreira, L., Lee, D., Chen, A., Schroeder, J.I., Balish, R.S., and Meagher, R.B. (2004). Overexpression of phytochelatin synthase in Arabidopsis leads to enhanced arsenic tolerance and cadmium hypersensitivity. Plant and Cell Physiology 45, 1787-1797. Li, Z.-S., Lu, Y.-P., Zhen, R.-G., Szczypka, M., Thiele, D.J., and Rea, P.A. (1997). A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalyzed transport of bis (glutathionato) cadmium. Proceedings of the National Academy of Sciences 94, 42-47. Maitani, T., Kubota, H., Sato, K., and Yamada, T. (1996). The composition of metals bound to class III metallothionein (phytochelatin and its desglycyl peptide) induced by various metals in root cultures of Rubia tinctorum. Plant Physiology 110, 1145-1150. Matsumoto, S., Shiraki, K., Tsuji, N., Hirata, K., Miyamoto, K., and Takagi, M. (2004). Functional analysis of phytochelatin synthase from Arabidopsis thaliana and its expression in Escherichia coli and Saccharomyces cerevisiae. Science and Technology of Advanced Materials 5, 377-381. Matsuura, H., Yamamoto, Y., Muraoka, M., Akaishi, K., Hori, Y., Uemura, K., Tsuji, N., Harada, K., Hirata, K., and Bamba, T. (2013). Development of surface‐engineered yeast cells displaying phytochelatin synthase and their application to cadmium biosensors by the combined use of pyrene‐excimer fluorescence. Biotechnology progress 29, 1197-1202. Mendoza‐Cózatl, D.G., Springer, F., Torpey, J.W., Komives, E.A., Kehr, J., and Schroeder, J.I. (2008). Identification of high levels of phytochelatins, glutathione and cadmium in the phloem sap of Brassica napus. A role for thiol‐peptides in the long‐distance transport of cadmium and the effect of cadmium on iron translocation. The Plant Journal 54, 249-259. Meuwly, P., Thibault, P., and Rauser, W.E. (1993). γ-Glutamylcysteinylglutamic acid-a new homologue of glutathione in maize seedlings exposed to cadmium. FEBS letters 336, 472-476. Ogawa, S., Yoshidomi, T., and Yoshimura, E. (2011). Cadmium (II)-stimulated enzyme activation of Arabidopsis thaliana phytochelatin synthase 1. Journal of inorganic biochemistry 105, 111-117. Ortiz, D., Kreppel, L., Speiser, D., Scheel, G., McDonald, G., and Ow, D. (1992). Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter. The EMBO journal 11, 3491. Ortiz, D.F., Ruscitti, T., McCue, K.F., and Ow, D.W. (1995). Transport of metal-binding peptides by HMT1, a fission yeast ABC-type vacuolar membrane protein. Journal of Biological Chemistry 270, 4721-4728. Park, J., Song, W.Y., Ko, D., Eom, Y., Hansen, T.H., Schiller, M., Lee, T.G., Martinoia, E., and Lee, Y. (2012). The phytochelatin transporters AtABCC1 and AtABCC2 mediate tolerance to cadmium and mercury. The Plant Journal 69, 278-288. Ramos, J., Clemente, M.R., Naya, L., Loscos, J., Pérez-Rontomé, C., Sato, S., Tabata, S., and Becana, M. (2007). Phytochelatin synthases of the model legume Lotus japonicus. A small multigene family with differential response to cadmium and alternatively spliced variants. Plant physiology 143, 1110-1118. Ray, D., and Williams, D.L. (2011). Characterization of the phytochelatin synthase of Schistosoma mansoni. PLoS neglected tropical diseases 5, e1168. Romanyuk, N.D., Rigden, D.J., Vatamaniuk, O.K., Lang, A., Cahoon, R.E., Jez, J.M., and Rea, P.A. (2006). Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase. Plant physiology 141, 858-869. Ruotolo, R., Peracchi, A., Bolchi, A., Infusini, G., Amoresano, A., and Ottonello, S. (2004). Domain Organization of Phytochelatin Synthase FUNCTIONAL PROPERTIES OF TRUNCATED ENZYME SPECIES IDENTIFIED BY LIMITED PROTEOLYSIS. Journal of Biological Chemistry 279, 14686-14693. Salt, D.E., and Rauser, W.E. (1995). MgATP-dependent transport of phytochelatins across the tonoplast of oat roots. Plant Physiology 107, 1293-1301. Slamet-Loedin, I.H., Johnson-Beebout, S.E., Impa, S., and Tsakirpaloglou, N. (2015). Enriching rice with Zn and Fe while minimizing Cd risk. Frontiers in plant science 6. Song, W.-Y., Park, J., Mendoza-Cózatl, D.G., Suter-Grotemeyer, M., Shim, D., Hörtensteiner, S., Geisler, M., Weder, B., Rea, P.A., and Rentsch, D. (2010). Arsenic tolerance in Arabidopsis is mediated by two ABCC-type phytochelatin transporters. Proceedings of the National Academy of Sciences 107, 21187-21192. Vögeli-Lange, R., and Wagner, G.J. (1990). Subcellular Localization of Cadmium and Cadmium-Binding Peptides in Tobacco Leaves Implication of a Transport Function for Cadmium-Binding Peptides. Plant Physiology 92, 1086-1093. Vatamaniuk, O.K., Mari, S., Lu, Y.-P., and Rea, P.A. (1999). AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution. Proceedings of the National Academy of Sciences 96, 7110-7115. Vatamaniuk, O.K., Mari, S., Lu, Y.-P., and Rea, P.A. (2000). Mechanism of heavy metal ion activation of phytochelatin (PC) synthase blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides. Journal of Biological Chemistry 275, 31451-31459. Vatamaniuk, O.K., Bucher, E.A., Ward, J.T., and Rea, P.A. (2001). A New Pathway for Heavy Metal Detoxification in Animals PHYTOCHELATIN SYNTHASE IS REQUIRED FOR CADMIUM TOLERANCE INCAENORHABDITIS ELEGANS. Journal of Biological Chemistry 276, 20817-20820. Vatamaniuk, O.K., Mari, S., Lang, A., Chalasani, S., Demkiv, L.O., and Rea, P.A. (2004). Phytochelatin Synthase, a Dipeptidyltransferase That Undergoes Multisite Acylation with γ-Glutamylcysteine during Catalysis STOICHIOMETRIC AND SITE-DIRECTED MUTAGENIC ANALYSIS OF ARABIDOPSIS THALIANA PCS1-CATALYZED PHYTOCHELATIN SYNTHESIS. Journal of Biological Chemistry 279, 22449-22460. Verbruggen, N., Hermans, C., and Schat, H. (2009). Molecular mechanisms of metal hyperaccumulation in plants. New Phytologist 181, 759-776. Vestergaard, M.d., Matsumoto, S., Nishikori, S., Shiraki, K., Hirata, K., and Takagi, M. (2008). Chelation of cadmium ions by phytochelatin synthase: role of the cystein-rich C-terminal. Analytical Sciences 24, 277-281. Yang, X., Feng, Y., He, Z., and Stoffella, P.J. (2005). Molecular mechanisms of heavy metal hyperaccumulation and phytoremediation. Journal of Trace Elements in Medicine and Biology 18, 339-353. Yong, X., Chen, Y., Liu, W., Xu, L., Zhou, J., Wang, S., Chen, P., Ouyang, P., and Zheng, T. (2014). Enhanced cadmium resistance and accumulation in Pseudomonas putida KT2440 expressing the phytochelatin synthase gene of Schizosaccharomyces pombe. Letters in applied microbiology 58, 255-261. Zhang, H., Zhou, H., Berke, L., Heck, A.J., Mohammed, S., Scheres, B., and Menke, F.L. (2013). Quantitative phosphoproteomics after auxin-stimulated lateral root induction identifies an SNX1 protein phosphorylation site required for growth. Molecular & Cellular Proteomics 12, 1158-1169. 王信傑. (2009). 植物螯合素合成酶催化機制研究. 博士論文 國立台灣大學 台北. 翁震炘. (2006). 農作物重金屬污染監測與管制措施. 農政與農情 169: 42-46 行政院農委會 台北. 張揚沛. (2014). 隱藏在食物中的危機－重金屬與神經疾病. 高醫醫訊月刊 33. 陳慎德. (2003). 淺論我國農地土壤重金屬汙染處理之現況與問題. 台灣土壤及地下水環境保護協會簡訊 9: 10-17 9, 7. 賈儒珍. (2014). 阿拉伯芥植物螯合素合成酶第二基質結合位及磷酸化後修飾之研究. 博士論文 國立台灣大學 台北. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/53589 | - |
| dc.description.abstract | 植物金屬螯合素合成酶 (phytochelatin synthase, PCS, EC2.3.2.15) 在植物對抗重金屬逆境時扮演著重要的角色。其利用兩種基質glutathione (GSH) 以及和金屬結合的glutathione衍生物 (Cd-GS2)，合成出具有金屬結合能力的植物螯合素 (phytochelatin, PC)，將重金屬螯合、隔離以降低重金屬對細胞的毒害。真核生物PCS的蛋白質結構可以分為主要催化活性區域的N端，以及含有多個Cys pair、為鎘離子主要結合區的C domain。目前的研究顯示，PCS在生物體內處於持續表現的狀態，但是只有當植物處於重金屬逆境下才能啟動其酵素活性，因此一般認為PCS之活性調節應是屬於轉譯後修飾 (post-translational modification) 之層級。本實驗室先前利用點突變技術以及酵母菌 (Pichia pastoris) 表現系統，發現阿拉伯芥 (Arabidopsis thaliana) AtPCS1 位於C端的Ser352是磷酸化修飾位點之一，對酵素活性也有顯著影響。Ser352在蛋白質一級序列上十分靠近C domain上的金屬結合位Cys358Cys359，本論文發現此磷酸化位點的突變不僅使酵素的活性降低，同時也會造成AtPCS1與金屬結合的比率上升。因此認為Ser352與金屬結合位Cys358Cys359之間可能存在著交互作用。進一步利用酵素動力學分析，發現將AtPCS1上的Ser352突變成Ala後，會使酵素對第一基質與第二基質的親和力大幅提升，但降低其催化速率。目前推測Ser352磷酸化位點會對AtPCS1產生綜合性影響，同時改變酵素對金屬之結合率。另一方面，本研究篩選於阿拉伯芥PCS缺失株cad1-3中分別表現AtPCS1或PCS-S352A之轉殖株。性狀分析結果顯示，4株PCS-S352A轉殖株之鎘耐受度與野生種均無明顯差距。綜合S352A 之生化性質與生理功能分析，本論文推測Ser352磷酸化修飾雖然會影響AtPCS1之酵素功能，但是在生理條件下酵素雖然只保留部分催化活性，但可能可以合成足夠的PC來維持植株在重金屬環境下之生長；而PCS本身也具有螯合重金屬的能力，在植物體內可能是一種優良的重金屬螯合分子，防止重金屬離子對細胞造成毒害。 | zh_TW |
| dc.description.abstract | Phytochelatin synthase (PCS, EC2.3.2.15) plays important roles in the sequestration of heavy metals in Arabidopsis thaliana. It uses two substrates, GSH and Cd-GS2, to synthesize phytochelatin (PC) via ping-pong mechanism. PC chelates heavy metals and forms a high molecular complex, which is then transferred to vacuoles to prevent from damaging the cells. PCS composes of a catalytic domain at N-terminus and a Cys-rich C-terminal domain which is responsive to cadmium (Cd). Many studies show that PCS is constitutively expressed in cytosol but could be only activated under heavy metal stress. The phenomenon indicates that PCS may be regulated by post-translational modification. Our previous data have demonstrated that recombinant AtPCS1 could be activated by in vitro phosphorylation. Furthermore, phosphorylation at Ser352 of recombinant AtPCS1 might affect the catalysis of the enzyme. Ser352 is close to Cys358Cys359, which is a heavy-metal binding site of the C-terminal domain. This study showed that mutation at Ser352 decreased the catalytic activity of PCS while increased the Cd binding ratio of the enzyme. Moreover, Recombinant AtPCS1 with a mutation at Ser352 showed a lower catalytic activity because of the significantly reduced Vmax along with the higher affinities to both substrates, which suggested the role of Ser352 in activation of PCS. On the other hand, this study selected 6 Arabidopsis transgenic lines that express AtPCS1 and AtPCS1-S352A in a PC-deficient mutant, cad1-3. Although S352A has a low catalytic activity in vitro, AtPCS1-S352A transgenic lines showed no significant changes in Cd tolerance comparing to the wild type Arabidopsis. Thus, we speculated that partially-activated PCS could synthesize enough PC to rescue the Cd tolerance of the transgenic lines, and the PCS might also act as a chelator to bind heavy metals in cytosol. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T02:26:04Z (GMT). No. of bitstreams: 1 ntu-104-R02b22051-1.pdf: 2216818 bytes, checksum: 071a1518cda47a2d6d20d7a52a5b6aac (MD5) Previous issue date: 2015 | en |
| dc.description.tableofcontents | 目錄 i
中文摘要 iv Abstract v 第一章 緒論 1 1.1重金屬與環境 1 1.1.2重金屬的定義 1 1.1.3重金屬的危害 1 1.1.4重金屬清除的方法 2 1.2植物對重金屬毒害的耐受性機制 3 1.2.1植物金屬螯合素 3 1.2.2植物金屬螯合素與金屬結合後在植物體內的儲存與運送方式 4 1.3植物金屬螯合素合成酶 5 1.3.1植物金屬螯合素合成酶基因序列 6 1.3.2植物金屬螯合素合成酶催化機制 6 1.3.3植物金屬螯合素合成酶與金屬的結合 8 1.3.4植物金屬螯合素合成酶的生理功能與基因工程上的運用 8 1.4植物金屬螯合素合成酶活性調控機制 9 1.4.1植物金屬螯合素合成酶可能受到磷酸化調控 9 1.5研究動機 10 第二章 材料與方法 11 2.1材料 11 2.1.1酵母菌 (Pichia pastoris) 表現系統 11 2.1.2植物材料 11 2.2阿拉伯芥種植與篩選 11 2.2.1種子消毒與低溫處理 11 2.2.2種子培養 11 2.2.3種子之土壤栽培 12 2.2.4種子之收集 12 2.2.5轉殖種子之抗生素篩選 12 2.3阿拉伯芥植物金屬螯合素合成酶重組蛋白質製備 12 2.3.1質體之轉型-酵母菌 (Pichia pastoris) 表現系統 12 2.3.2阿拉伯芥植物金屬螯合素合成酶重組蛋白之表現 13 2.3.3阿拉伯芥植物金屬螯合素合成酶重組蛋白純化 13 2.4阿拉伯芥植物金屬螯合素合成酶和鎘結合之比例 14 2.4.1平衡透析法 14 2.4.2鎘離子的測定 14 2.4.4阿拉伯芥植物金屬螯合素合成酶與鎘之結合比例計算 14 2.5阿拉伯芥植物金屬螯合素合成酶重組蛋白之催化機制探討 15 2.5.1決定最適酵素反應濃度 15 2.5.2阿拉伯芥植物金屬螯合素合成酶重組蛋白質之活性分析 15 2.5.3 阿拉伯芥植物金屬螯合素合成酶重組蛋白質之酵素動力學 15 2.6 AtPCS1重組蛋白磷酸化染色實驗 16 2.6.1表現蛋白質去磷酸化處理 16 2.6.2 Pro-Q diamond染色法 16 2.7阿拉伯芥轉殖株蛋白質表現之確認 17 2.8阿拉伯芥轉殖株外表型 (phenotype) 之觀察 17 第三章 結果與討論 18 3.1 Ser352磷酸化位點突變株磷酸化程度分析 18 3.2 AtPCS1-Ser352磷酸化位點突變之酵素活性分析 18 3.3磷酸化位點Ser352突變後對鎘的結合比例改變 18 3.4以酵素動力學剖析Ser352於活性催化的角色 19 3.5以阿拉伯芥補償性轉殖株分析Ser352在生理上所扮演的角色 20 3.5.1阿拉伯芥補償性轉殖株抗生素之篩選 20 3.5.2轉殖株之PCS蛋白質表現量 21 3.5.3 阿拉伯芥植株重金屬處理之條件測試 21 3.5.4阿拉伯芥補償性轉殖株重金屬處理之表現型觀察 22 3.6 未來研究方向 25 參考文獻 48 問答錄 54 | |
| dc.language.iso | zh-TW | |
| dc.subject | 磷酸化位點Ser352 | zh_TW |
| dc.subject | 植物金屬螯合素 | zh_TW |
| dc.subject | 植物金屬螯合素合成? | zh_TW |
| dc.subject | Phosphorylation site Ser352 | en |
| dc.subject | Phytochelatin synthase | en |
| dc.subject | Phytochelatin | en |
| dc.title | 阿拉伯芥植物金屬螯合素合成酶磷酸化後修飾位點Ser352之研究 | zh_TW |
| dc.title | Characterization of Ser352 phosphorylation site in Arabidopsis phytochelatin synthase | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 103-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 陳翰民,楊健志,吳裕仁,張世宗 | |
| dc.subject.keyword | 植物金屬螯合素,植物金屬螯合素合成?,磷酸化位點Ser352, | zh_TW |
| dc.subject.keyword | Phytochelatin,Phytochelatin synthase,Phosphorylation site Ser352, | en |
| dc.relation.page | 58 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2015-08-05 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科技學系 | zh_TW |
| 顯示於系所單位： | 生化科技學系 | |
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| ntu-104-1.pdf 未授權公開取用 | 2.16 MB | Adobe PDF |
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