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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
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dc.contributor.advisor | 莊榮輝(Rong-Huay Juang) | |
dc.contributor.author | Chih-yi Lin | en |
dc.contributor.author | 林之儀 | zh_TW |
dc.date.accessioned | 2021-05-20T20:17:41Z | - |
dc.date.available | 2009-07-14 | |
dc.date.available | 2021-05-20T20:17:41Z | - |
dc.date.copyright | 2009-07-14 | |
dc.date.issued | 2009 | |
dc.date.submitted | 2009-07-01 | |
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Faseb J 6: 2274-2282 Kossmann J, Visser RG, Muller-Rober B, Willmitzer L, Sonnewald U (1991) Cloning and expression analysis of a potato cDNA that encodes branching enzyme: evidence for co-expression of starch biosynthetic genes. Mol Gen Genet 230: 39-44 Lao NT, Schoneveld O, Mould RM, Hibberd JM, Gray JC, Kavanagh TA (1999) An Arabidopsis gene encoding a chloroplast-targeted beta-amylase. Plant J 20: 519-527 Liu TT, Shannon JC (1981) A Nonaqueous Procedure for Isolating Starch Granules with Associated Metabolites from Maize (Zea mays L.) Endosperm. Plant Physiol 67: 518-524 Mori H, Tanizawa K, Fukui T (1991) Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide sequence, and expression of a full-length cDNA in Escherichia coli. J Biol Chem 266: 18446-18453 Mori H, Tanizawa K, Fukui T (1993) A Chimeric Alpha-Glucan Phosphorylase of Plant Type-L and Type-H Isozymes - Functional-Role of 78-Residue Insertion in Type-L Isozyme. J Biol Chem 268: 5574-5581 Mouille G, Maddelein ML, Libessart N, Talaga P, Decq A, Delrue B, Ball S (1996) Preamylopectin Processing: A Mandatory Step for Starch Biosynthesis in Plants. Plant Cell 8: 1353-1366 Nelson O, Pan D (1995) Starch Synthesis in Maize Endosperms. Annu Rev Plant Physiol Plant Mol Biol 46: 475-496 Ohdan T, Francisco PB, Jr., Sawada T, Hirose T, Terao T, Satoh H, Nakamura Y (2005) Expression profiling of genes involved in starch synthesis in sink and source organs of rice. J Exp Bot 56: 3229-3244 Okita TW, Greenberg E, Kuhn DN, Preiss J (1979) Subcellular-Localization of the Starch Degradative and Biosynthetic-Enzymes of Spinach Leaves. Plant Physiol 64: 187-192 Preiss J, Okita TW, Greenberg E (1980) Characterization of the Spinach Leaf Phosphorylases. Plant Physiol 66: 864-869 Ritte G, Raschke, K. (2003) Metabolite export of isolated guard cell chloroplasts of Vicia faba. 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In the 'The biochemistry of plants' Academia Press. New York 14: 255-296 Steup M, Latzko E (1979) Intracellular-Localization of Phosphorylases in Spinach and Pea Leaves. Planta 145: 69-75 Tetlow IJ, Morell MK, Emes MJ (2004) Recent developments in understanding the regulation of starch metabolism in higher plants. J Exp Bot 55: 2131-2145 Tsai CY, Nelson OE (1968) Phosphorylases I and II of Maize Endosperm. Plant Physiol 43: 103-112 Weise SE, Weber AP, Sharkey TD (2004) Maltose is the major form of carbon exported from the chloroplast at night. Planta 218: 474-482 Wirtz W, Stitt M, Heldt HW (1980) Enzymic Determination of Metabolites in the Subcellular Compartments of Spinach Protoplasts. Plant Physiol 66: 187-193 Yan L, Jon, M. S., Jian, Y., and Thomas, D. S. (2006) The Role of Cytosolic a-Glucan Phosphorylase in Maltose Metabolism and the Comparison of Amylomaltase in Arabidopsis and Escherichia coli. Plant Physiol 142: 878-889 Yang Y, Steup M (1990) Polysaccharide Fraction from Higher Plants which Strongly Interacts with the Cytosolic Phosphorylase Isozyme : I. Isolation and Characterization. Plant Physiol 94: 960-969 Yu Y, Mu, H. H., Wasserman, B. P., and Carman, G. M. (2001) Identification of the Maize Amyloplast Stromal 112-kD Protein as a Plastidic Starch Phosphorylase and structure of starch in the endosperm. Plant Physiol 125: 351-359 Zeeman SC, Umemoto T, Lue WL, Au-Yeung P, Martin C, Smith AM, Chen J (1998) A mutant of Arabidopsis lacking a chloroplastic isoamylase accumulates both starch and phytoglycogen. Plant Cell 10: 1699-1712 王宏祥 (2007) 甘藷塊根澱粉磷解脢不需醣引子活性之分子機制探討. 碩士論文 國立台灣大學 台北 王維德 (2006) L78 對L 型澱粉磷解酶活性調控及催化機制之角色. 碩士論文 國立台灣大學 台北 吳其真 (1998) 甘藷澱粉磷解脢之生化及免疫學研究. 碩士論文 國立台灣大學 台北 陳翰民 (1997) 甘藷澱粉磷解脢構造與功能之研究. 博士論文 國立台灣大學 台北 曾光靖 (2005) 磷酸化修飾對甘藷塊根L型澱粉磷解脢之影響. 碩士論文 國立台灣大學 台北 楊光華 (2005) 甘藷塊根澱粉磷解脢激脢之純化與性質分析. 博士論文 國立臺灣大學 台北 | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/9326 | - |
dc.description.abstract | L型澱粉磷解酶 (L-SP) 為存在於高等植物造粉體之澱粉代謝酵素,同時具有磷解澱粉以及合成澱粉雙方向之活性。在in vitro可以利用基質Glc-1-P於不含醣引子 (primer-independent, PI) 或者是含醣引子 (primer-dependent) 之情況下進行直鏈醣合成。使用HPAEC (high performance anion exchange chromatograph) 分析發現,L-SP的PI反應之速率決定步驟為將兩個單醣合成雙醣,而當Glc-1-P合成雙醣或寡醣後,反應即進入快速延長時期,此時磷酸釋放以及直鏈醣生成速率皆大幅上升。此外,本論文發現在L-SP上與Glc-1-P結合的兩個區域,其中之一對於基質辨認之專一性較高,僅能與Glc-1-P結合 (在活性區上);另一個結合區可能在L-SP之特殊插入序列L78上,可接受不同的基質,故可與Glc-1-P以外之六碳醣磷酸結合。利用L-SP之同功酶H-SP進行不含醣引子之合成反應,發現其不具PI之活性。由上述結果推論,L-SP之催化機制應該是由PLP (pyridoxal phosphate) 結合區上之Glc-1-P先裂解生成碳陽離子後,再去攻擊與L78結合之第二個Glc-1-P的非還原端,形成 | zh_TW |
dc.description.abstract | L-Form starch phosphorylase (L-SP) is a plastidial alpha-glucan phosphorylase in higher plants which catalyzes reversible reactions of starch synthesis and degradation. In vitro, the enzyme might synthesize linear glucan in the absence of a primer (primer-independent activity, PI activity). By analyzing glucan products with HPAEC (high performance anion exchange chromatograph), we found that the rate-determining step in the PI activity was the formation of disaccharide from two molecules of Glc-1-P. The reaction went into rapid elongation phase after disaccharides or oligosaccharides were produced. At this stage, the rate of the phosphate releasing and linear glucan synthesizing increased exponentially. In each cycle of catalytic reaction, one Glc-1-P bound to the active site on L-SP with high affinity which was then reacted with the other molecule of Glc-1-P on L78, the insertion region on L-SP. The basic amino acids on L78 could bind with Glc-1-P or short glucan to serve as the second substrate binding site. It was postulated that the catalytic mechanism for L-SP might follow these steps: The Glc-1-P anchored to PLP (pyridoxal phosphate) in binding site and was cleaved into carbocation, then attacked the nonreducing end of the second Glc-1-P or glucan on L78, forming | en |
dc.description.provenance | Made available in DSpace on 2021-05-20T20:17:41Z (GMT). No. of bitstreams: 1 ntu-98-R96b47208-1.pdf: 3412180 bytes, checksum: 0608aed09e7128c3d6ff1d0886a6c829 (MD5) Previous issue date: 2009 | en |
dc.description.tableofcontents | 目錄 I
中文摘要 III Abstract IV 第一章 緒論 1 1.1 alpha 型葡聚醣磷解酶 1 1.1.1 澱粉磷解酶 1 1.1.2 植物澱粉磷解酶與動物肝醣磷解酶之比較 2 1.1.3 植物L型澱粉磷解酶及H型澱粉磷解酶之比較 2 1.2 澱粉代謝 7 1.2.1 澱粉 7 1.2.2 澱粉之代謝途徑 7 1.3 L 型澱粉磷解酶之生理角色 11 1.3.1 磷解澱粉 11 1.3.2 合成澱粉 11 1.3.3 不需醣引子合成直鏈醣之活性 12 1.3.4 H 型澱粉磷解酶之生理角色 14 1.4 實驗室目前相關研究進度 16 1.5 研究動機 17 第二章 材料與方法 21 2.1 基本分析法 21 2.1.1 Bradford 定量法 21 2.1.2 酵素活性分析 (不含醣引子) 22 2.1.3 酵素活性分析 (添加醣引子) 23 2.2 澱粉磷解酶純化法 25 2.2.1 粗抽取及硫酸銨分劃 25 2.2.2 離子交換法 27 2.2.3 疏水性層析法 28 2.2.4 膠體過濾法 29 2.3 電泳檢定法 31 2.3.1 原態膠體電泳 31 2.3.2 SDS 膠體電泳 34 2.3.3 膠片染色法 36 2.3.3.1 Coomassie Brilliant Blue R (CBR) 染色法 36 2.3.3.2 澱粉磷解脢活性染色法 36 2.3.4 膠片乾燥及護貝 38 2.4 醣類分析法 40 2.4.1 高效能液相層析法 40 2.4.2 高效能陰離子交換層析法 41 第三章 結果與討論 43 3.1 酵素之製備 43 3.1.1 甘藷塊根L型澱粉磷解酶製備 43 3.1.2 甘藷塊根H型澱粉磷解酶製備 44 3.2 L-SP 合成直鏈醣之模式 50 3.2.1 L-SP 不需醣引子合成醣前體活性 50 3.2.2 以 HPLC 測定 L-SP 利用不同短鏈醣合成直鏈醣之情形 50 3.2.3 以 HPAEC-PAD 分析三相反應之產物 55 3.2.4 Glc-1-P 的異構物對 L-SP 不需醣引子合成直鏈醣活性之影響 60 3.3 L-SP 與 H-SP 生化特性之異同 63 3.3.1 H-SP 不需醣引子合成直鏈醣活性 63 第四章 結論 66 參考文獻 68 問答錄 72 | |
dc.language.iso | zh-TW | |
dc.title | 甘藷塊根L型澱粉磷解酶不需醣引子合成醣前體之活性催化機制 | zh_TW |
dc.title | The Catalytic Mechanism of Primer-independent Glucan Precursor-Synthesizing Activity of L-Form Starch Phosphorylase from Sweet Potato Roots | en |
dc.type | Thesis | |
dc.date.schoolyear | 97-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 林棋財,陳翰民,楊健志,張世宗 | |
dc.subject.keyword | 澱粉磷解酶,澱粉代謝,不含醣引子合成,葡萄糖-1-磷酸,高效能陰離子交換層析法,磷酸吡,哆醛, | zh_TW |
dc.subject.keyword | starch phosphorylase,starch synthesis,primer-independent,PI,Glc-1-P,HPAEC-PAD,PLP, | en |
dc.relation.page | 78 | |
dc.rights.note | 同意授權(全球公開) | |
dc.date.accepted | 2009-07-01 | |
dc.contributor.author-college | 生命科學院 | zh_TW |
dc.contributor.author-dept | 微生物與生化學研究所 | zh_TW |
顯示於系所單位: | 微生物學科所 |
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