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DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Yen-Ju Chen | en |
dc.contributor.author | 陳晏如 | zh_TW |
dc.date.accessioned | 2021-07-01T08:20:53Z | - |
dc.date.available | 2021-07-01T08:20:53Z | - |
dc.date.issued | 1998 | |
dc.identifier.citation | 莊榮輝(1985)水稻蔗糖合?之研究。國立台灣大學農業化學研究所博士論文。 黃冠博(1993)水稻銅鋅超氧歧化?的cDNA選殖與性質研究。國立台灣大學植物科學研究所碩士論文。 潘素美(1995)植物如何因應環境變遷—超氧歧化?。氣候變遷與農業生產。楊盛行編。pp.119-134。中國農業化學會與行政院農業委員會印行。 劉宏基(1997)水稻銅鋅超氧歧化?之表達、純化與性質研究。國立台灣大學植物研究所碩士論文。 陳銘坤(1998)阿拉伯芥表現水稻超氧歧化?之研究。國立台灣大學植物科學研究所碩士論文。 Almansa, M.S., del Rio, L.A., Alcaraz, C.F. and Sevilla, F. (1989) Isoenzyme pattern of superoxide dismutase in different varieties of citrus plants. Physiol. Plant. 76: 563-568. Aono, M., Kubo, A., Saji, T.N., Tanaka, K. and Kondo, N. (1991) Resistance to active oxygen toxicity of transgenic Nicotiana tabacum that expresses the gene for glutathione reductase from Escherichia coli. Plant Cell Physiol. 32(5): 691-697. Beauchamp, C. and Fridovich, I. (1971) Superoxide dismutases: improved assays and an assay applicable to acrylamide gel. Anal. Biochem. 44: 276-287. Beyer, W., Imlay, J. and Fridovich, I. (1991) Superoxide dismutases. Prog. Nucl. Acid Res. Mol. Biol. 40: 221-248. Blum, H., Beier, H. and Gross, H.J. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8: 93-99. Bowler, C., Van Montagu, M. and Inz?, D. (1992) Superoxide dismutase and stress tolerance. Annu. Rev. Plant Physiol. Plant Mol. Biol. 43: 83-116. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254. Brawn, K. and Fridovich, I. (1981) DNA strand scission by enzymatically-generated oxygen radicals. Arch. Biochem. Biophys. 206: 414-419. Bray, R.C., Cockle, S.A., Fielden, E.M., Roberts, P.B., Rotulio, G. and Calabrese, L. (1974) Reduction and inactivation of superoxide dismutase by hydrogen peroxide. Biochem. J. 139: 43-48. Callis, J. (1995) Regulation of Protein Degradation. Plant Cell 7: 845-857. Ciriolo, M.R., Civitareale, P., Carri, M.T., Martino, A.D., Galiazzo, F. and Rotilio, G. (1994) Purification and characterization of Ag, Zn-superoxide dismutase from Saccharomyces cerevisiae exposed to silver. J. Biol. Chem. 269: 25783-25787. Deshaies, R.J., Koch, B.D. and Shekman, R. (1988) The role of stress proteins in membrane biogenesis. Trends Biochem. Sci. 13: 384-388. Ellis, R.E., Yuan, J. and Horvitz, H.R. (1991) Mechanisms and functions of cell death. Annu. Rev. Cell Biol. 7: 663-698. Fester, T. and Schuster, W. (1995) Potato mitochondrial manganese superoxide dismutase is an RNA-binding protein. Biochem. Mol. Biol. Int. 36: 67-75. Finley, D. and Chau, V. (1991) Ubiquitination. Annu. Rev. Cell Biol. 7: 25-69. Fridovich, I. (1975) Superoxide dismutases. Annu. Rev. Biochem. 44: 147-159. Fridovich, I. (1978) The biology of oxygen radicals. Science 201: 875-880. Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. pp. 649. Cold Spring Harbor Laboratory Press, USA. Hass, M.A. and Massaro, D. (1987) Developmental regulation of rat lung copper, zinc-superoxide dismutase. Biochem. J. 246(3): 697-704. Hodgson, E.K. and Fridovich, I. (1975) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme. Biochemistry 14: 5294-5303. Holmsen, T.W. and Koch, A.L. (1964) Phytochemistry 3: 165-172. Huffaker, R.C. and Peterson, L.W. (1974) Protein turnover in plants and possible means of its regulation. Annu. Rev. Plant Physiol. 25: 363-392. Jabs, T., Dietrich, R.A. and Dang, J.L. (1996) Initiation of runaway cell death in an Arabidopsis mutation by extracellular superoxide. Science 273: 1853-1856. Kanematsu, S. and Asada, K. (1989) CuZn-Superoxide dismutase in rice: occurrence of an active, monomeric enzyme and two types of isozyme in leaf and non-photosynthetic tissues. Plant Cell Physiol. 30: 381-391. Karlsson, K., Sandstrom, J., Edlund, A. and Marklund, S.L. (1994) Turnover of extracellular-superoxide dismutase in tissues. Laboratory Investigation 70: 705-710. Karpinski, S., Wingsles, G., Olsson, O. and H?llgren, J-E. (1992) Characterization of cDNAs encoding CuZn-superoxide dismutase in Sots pine. Plant Mol. Biol. 18: 545-555. Kitagawa, Y., Tanaka, N., Hata, Y., Kusunoki, M., Lee, G.P., Katsube. Y., Asade. K., Aibara, S. and Morita, Y. (1991) Three-dimensional structure of Cu, Zn-superoxide dismutase from spinach at 2.0 ? resolution. J. Biochem. 109: 477-485. Klerk, H. and Van Loon, L.C. (1997) Charcteristics of protein turnover in the developing first leaf of oats (Avena sativa L.). J. Plant Physiol. 15: 176-187. Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of bacteriophage T4. Nature 227: 680-685. Matile, P.H. (1982) Protein degradation. In Encyclopedia of Plant Physiology. New Ser. 14A: 169-188. Berlin: Springer-Verlag. Mattoo, A.K., Hoffman-Falk, H., Marder, J.B., Edelman, M. (1984) Regulation of protein metabolism: coupling of photosynthetic electron transport to the in vivo degradation of the rapidly metabolized 32-kilodalton protein in the chloroplast membranes. Proc. Natl. Acad. Sci. USA 81: 1380-1384. Maurizi, M.R. (1992) Proteases and protein degradation in Escherichia coli. Experientia 48: 178-201. McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244: 6049-6055. Meier, B., Sehn, A.P., Sette, M., Paci, M., Desider, A. and Rotilto, G. (1994) In wiwo incorporation of cobalt into Propionibacterium shermanii superoxide dismutases. FEBS Lett 348: 283-286. Mothes, K. (1993) Investigation on the assimilation of ammonia. Planta 19: 117-138. O’Farrell, P.H. (1975) High resolution two-dimensional eletrophoresis of proteins. J. Biol. Chem. 250: 4007-4021. Oliver, S.C., Venis, M.A., Freedman, R.B., Napier, R.M. (1995) Regulation of synthesis and turnover of maize auxin-binding protein and observations on its passage to the plasma membrane: comparisons to maize immunoglobulin-binding protein cognate. Planta 197: 465-474. Pan, S.M. and Yau, Y.Y. (1991) The isozymes of superoxide dismutase in rice. Bot. Bull. Acad. Sin. 32: 253-258. Pell, E.J. and Steffen, K.L. (1991) Active oxygen/oxidative stress and plant metabolism. In Current Topics in Plant Physiology. An American Society of Plant Physiologists, series Vol. 6. Poole, B., Leighton, F., and de Duve, C. (1969) J. Cell Biol. 41: 536-546. Rice-Evans, C.A., Miller, N.J. and Paganga, G. (1997) Antioxidant properties of phenolic compounds. Trends in Plant Sci. 2: 152-159. Richardson, J.S., Thomas, K.A., Rybin, J.H. and Richardson, D.C. (1975) Crystal structure of bovine CuZn superoxide dismutase at 3 ? resolution: Chain tracing and metal ligands. Proc. Natl. Acad. Sci. USA 72:1349-1353. Rogers, S., Wells, R. and Rechsteiner, M. (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368. Sakamoto, A., Ohsuga, H., Wakaura, M., Mitsukawa, N., Hibino, T., Masumura, T., Sasaki, Y. and Tanaka, K. (1990) Nucleotide sequence of cDNA for the cytosolic Cu/Zn-superoxide dismutase from spinach (Spinacia oleraceaee L.). Nucleic Acids Res. 18: 4923. Sakamoto, A., Nosaka, Y. and Tanaka, K. (1993) Cloning and sequencing analysis of a complementary DNA for manganese-superoxide dismutase from rice (Oryza sativa L.). Plant Physiol. 103: 1477-1478. Sambrook, J., Fritsch, E.R. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory Press, USA. Scandalios, J.G. (1992) Molecular biology of free radical scavenging systems. Cold Spring Harber Laboratory, Cold Spring Harber, New York. Scandalios, J.G. (1993) Oxygen stress and superoxide dismutases. Plant Physiol. 101: 7-12. Seglen, P.O. and Bohley, P. (1992) Autophagy and other vacuolar protein degradation mechanisms. Experientia 48: 158-172. Sen Gupta, A., Webb, R.P., Holaday, A.S. and Allen, R.D. (1993) Overexpression of superoxide dismutase protects plants from oxidative stress. Plant Physiol. 103: 1067-1073. Seufert, W. and Jentsch, S. (1990) Ubiquitin conjugation enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9: 543-550. Sevilla, F., L?pze-Gorg?, J., G?mez, M. and del Rio, L.A. (1980) Manganese superoxide dismutase from a higher plant. Planta 150: 153-157. Slooten, L., Capiau, K., Van camp, W., Van Montagu, M., Sybesma, C. and Inz?, D. (1995) Factors affecting the enhancement of oxidative stress tolerance in transgenic tobacco overexpressing manganese superoxide dismutase in the chloroplasts. Plant Physiol. 107: 737-750. Tainer, J.A., Getzoff, E.D., Beem, K.M., Richardson, J.S. and Richardson, D.C. (1982) Determination and analysis of the 2 ? structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160: 181-217. Tainer, J.A., Getzoff, E.D., Richardson, J.S. and Richardson, D.C. (1983) Structure and mechanism of copper, zinc superoxide dismutase. Nature 306: 284. Varshavsky, A. (1992) The N-end rule. Cell 69: 725-735. Vierstra, R.D. (1993) Protein degradation in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 44: 385-410. Wang, X., Culotta, V.C. and Klee, C.B. (1996) Superoxide dismutase protects calcineurin from inactivation. Nature 383: 434-437. White, J.A. and Scandalios, J.G. (1988) Isolation and characterization of a cDNA for mitochondrial manganese superoxide dismutase (SOD-3) of maize and its relation to other manganese superoxide dismutases. Biochim. Biophys. Acta 951: 61-70. Zielke, H.R. and Filner, P. (1971) Synthesis and turnover of nitrate reductase induced by nitrate in cultured tobacco cells. J. Biol. Chem. 246: 1772-1779. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76379 | - |
dc.description.abstract | 以大量表現水稻銅鋅超氧歧化?(CuZnSOD)之阿拉伯芥轉殖株和野生株為材料,利用單向電泳法來分析野生株和轉殖株之蛋白質,發現除了轉殖基因產物水稻CuZnSOD之外,兩者之蛋白質含量及種類大致相同。以雙向電泳法分析其蛋白質及西方點墨分析,則發現轉殖株至少多了5個pI值不同但分子量相同可被水稻CuZnSOD抗體所辨認之額外蛋白質。取阿拉伯芥之葉柄進行35S-methionine活體標定之實驗,結果顯示野生株及轉殖株對於35S-methionine皆有21-29%的吸收率,約有1?1.5%進入新合成的蛋白質。萃取之蛋白質利用電泳分析和自動放射顯影技術,分析其標定期間新合成之蛋白質,轉殖株中大部份蛋白質的衰變與野生株相似,而轉殖基因表現之CuZnSOD其衰變速度較大部份蛋白質為快。若以單向電泳分析則水稻之CuZnSOD於轉殖株葉片中約20小時之內可衰變50%的量。本論文並討論以35S-methionine活體標定葉片後再以雙向電泳分析CuZnSOD之衰變結果。 | zh_TW |
dc.description.abstract | In order to estimate the turnover of CuZn-superoxide dismutase (CuZnSOD) and the gene products in transgenic Arabidopsis, protein patterns of SOD-overexpressor and wild-type plants from Arabidopsis Columbia ecotype were analyzed by 1 D-PAGE or 2D-PAGE. After the pulse and chase experiment with 35S-methionine was done in the shoot parts of plants, the soluble polypeptides from the leaves were extracted. The de novo polypeptides were analyzed with one- or two-dimensional gel electrophoresis and autoradiography. The uptake of 35S-methionine and incorporation into polypeptides in the transgenic Arabidopsis were about 21?29% and 1.5%, respectively, which were similar to those observed in the wild-type plants. The turnover of rice CuZnSOD in SOD-transgenic Arabidopsis was estimated to be within 20 hr by the 1D-PAGE and autoradiogram image analysis. 2D-PAGE and autoradiogram image analysis were also used and discussed in the turnover study of CuZnSOD in SOD-transgenic Arabidopsis. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:20:53Z (GMT). No. of bitstreams: 0 Previous issue date: 1998 | en |
dc.description.tableofcontents | 縮寫表……………………………………………………I 中文摘要……………………………………………………III 英文摘要……………………………………………………IV 第一章 前言…………………………………………………………………………………………………………1 第一節 研究緣起………………………………………………………………………………………………1 第二節 前人的研究……………………………………………………………………………………………1 第一項 活性氧分子的產生及其影響……………………………………………………………………1 第二項 生物之抗氧化機制與SOD的功能 ………………………………………………………………3 第三項 植物中蛋白質的衰變……………………………………………………………………………6 第四項 SOD之衰變研究 …………………………………………………………………………………9 第二章 材料與方法…………………………………………………………………………………………………10 第一節 實驗材料………………………………………………………………………………………………10 第二節 活體蛋白質標定………………………………………………………………………………………10 第三節 植物總蛋白質的萃取…………………………………………………………………………………11 第一項 總蛋白質之萃取…………………………………………………………………………………12 第二項 放射性同位素標定後之植物總蛋白質的萃取(少量材料)…………………………………13 第四節 蛋白質的定量…………………………………………………………………………………………13 第一項 不含urea或SDS之樣品 …………………………………………………………………………14 第二項 含urea或SDS之樣品 ……………………………………………………………………………15 第五節 聚丙烯醯胺膠體電泳…………………………………………………………………………………16 第一項 SDS膠體電泳 ……………………………………………………………………………………16 第二項 蛋白質雙向電泳分析……………………………………………………………………………19 第六節 COOMASSIE BRILLIANT BLUE R-250 (CBR)染色法…………………………………………………22 第七節 硝酸銀染色法…………………………………………………………………………………………23 第八節 蛋白質放射性強度判讀………………………………………………………………………………25 第九節 西方點墨法……………………………………………………………………………………………25 第十節 蛋白質放射性強度的測試……………………………………………………………………………29 第三章 結果…………………………………………………………………………………………………………30 第一節 阿拉伯芥葉片對35S-METHIONINE之吸收及新合成蛋白質之標定…………………………………30 第二節 轉殖株中水稻CUZNSOD及其它蛋白質之表現 ………………………………………………………35 第三節 轉殖株中水稻CUZNSOD蛋白質之衰變 ………………………………………………………………42 第四章 討論…………………………………………………………………………………………………………48 第一節 阿拉伯芥蛋白質活體標定系統的建立………………………………………………………………48 第二節 轉殖株中水稻CUZNSOD之表現 ………………………………………………………………………50 第三節 蛋白質衰變情形之研究………………………………………………………………………………51 參考文獻 ……………………………………………………………………………………………………………54 | |
dc.language.iso | zh-TW | |
dc.title | 水稻銅鋅超氧歧化?在阿拉伯芥轉殖株葉中其蛋白質衰變之研究 | zh_TW |
dc.title | Turnover of Rice CuZnSOD in the Leaves of SOD-Overexpressing Arabidopsis | en |
dc.date.schoolyear | 86-2 | |
dc.description.degree | 碩士 | |
dc.relation.page | 61 | |
dc.rights.note | 未授權 | |
dc.contributor.author-dept | 生命科學院 | zh_TW |
dc.contributor.author-dept | 植物科學研究所 | zh_TW |
顯示於系所單位: | 植物科學研究所 |
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