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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 莊榮輝 | |
| dc.contributor.author | Chun-li Wang | en |
| dc.contributor.author | 王群力 | zh_TW |
| dc.date.accessioned | 2021-06-13T16:30:14Z | - |
| dc.date.available | 2005-07-15 | |
| dc.date.copyright | 2005-07-15 | |
| dc.date.issued | 2005 | |
| dc.date.submitted | 2005-07-12 | |
| dc.identifier.citation | 陳翰民 (1997) 甘藷澱粉磷解脢構造與功能之研究
國立台灣大學農業化學研究所博士論文 張世宗 (1999) 甘藷塊根Chaperonin及Proteosome之分離與性質研究 國立台灣大學農業化學研究所博士論文 楊光華 (2005) 甘藷塊根澱粉磷解脢激脢之純化與性質分析 國立台灣大學農業化學研究所博士論文 Albrecht T, Greve B, Pusch K, Kossmann J, Buchner P, Wobus U, Steup M (1998) Homodimers and heterodimers of Pho1-type phosphorylase isoforms in Solanum tuberosum L. as revealed by sequence specific antibodies. Eur J Biochem 251: 343-352 Albrecht T, Koch A, Lode A, Greve B, Schneider-Margener J, Steup M (2001) Plastidic (Pho1-type) phosphorylase isoforms in potato (Solanum tuberosum L.) plants: expression analysis and immunochemical characterization. Planta 213: 602-613 Ball SG, Guan H, James M, Myers A, Keeling P, Mouille G, Buléon A, Colonna P, Preiss J (1996) From glycogen to amylopectin: a model for the biogenesis of the plant starch granule. Cell 86: 349-352 Berwick DC, Tavaré JM (2004) Identifying protein kinase substrates: hunting for the organ-grinder’s monkeys. Trends Biochem. Sci. 29: 227-232 Blom N, Gammeltoft S, Brunak S (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294: 1351-1362 Brinkworth RI, Breinl RA, Kobe B (2003) Structural basis and prediction of substrate specificity in protein serine/threonine kinases. Proc. Natl. Acad. Sci. USA. 100: 74-79 Burton RA, Bewley JD, Smith AM, Bhattacharyya MK, Tatge H, et al. (1995) Starch branching enzymes belonging to distinct enzyme families are differentially expressed during pea embryo development. Plant J. 7: 3-15 Commuri PD, Keeling PL (2001) Chain-length specificities of maize starch synthase I enzyme: studies of glucan affinity and catalytic properties. Plant J. 25: 475-486 Chen HM, Chang SC, WU CC, Cuo TS, Wu JS, Juang RH (2002) Regulation of the catalytic behaviour of L-form starch phosphorylase from sweet potato roots by proteolysis. Physiol. Plant. 114: 506-515 de Fekete MAR, Leloir LF, Cardini CE (1960) Mechanism of starch biosynthesis. Nature 187: 918-919 de Fekete MAR, Vieweg GH (1973) The role of phosphorylase in the metabolism of starch. Ann. N Y Acad. Sci. 210: 170-180 Frydman RB, Cardini CE (1964) Biosynthesis of phytoglycogen from adenosine diphosphate D-glucose in sweet corn. Biochem. Biophys. Res. Commun. 14: 353-357 Fukui T (1983) Plant phosphorylase: structure and function. In T Akazawa, T Asahi, He Imaseki, eds, The New Frontiers in Plant Biochemistry, Ed Japan Scientific Societies Press Tokyo, pp 71-82 Geigenberger P (2003) Regulation of sucrose to starch conversion in growing potato tubers. J. Exp. Botany 382: 457-465 Guan HP, Preiss J (1993) Differentiation of the properties of the branching isozymes form maize (Zea mays) Plant Physiol. 102: 1269-73 Hanes CS (1940) The reversible formation of starch from glucose-1-phosphate catalyzed by potato phosphorylase. Proc. R. Soc. (London) B129: 174-208 Hardin SC, Huber SC (2004) Proteasome activity and the post-translational control of sucrose synthase stability in maize leaves. Plant Physiol. Biochem. 42: 197-208 Jenkins PJ, Cameron RE, Donald AM (1993) A universal feature in the starch granules from different botanical sources. Starke 45: 417-420 Johnson LN, Barford D (1990) Glycogen phosphorylase. The structural basis of the allosteric response and comparison with other allosteric proteins. J. Biol. Chem. 265: 2409-2412 Kuriki T, Stewart DC, Preiss J (1997) Construction of chimeric enzymes out of maize endosperm branching enzyme I and II: activity and properties. J. Biol Chem. 272: 28999-29004 Larsson C-T, Hofvander P, Khoshnoodi J, Ek B, Rask L, Larsson H (1996) Three isoforms of starch-branching enzyme are present in potato tuber. Plant Sci. 117: 9-16 Mann M, Jensen ON (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21: 255-561 Merida A, Rodriguez-Galan JM, Vincent C, Romero JM (1999) Expression of the granule-bound starch synthase I (Waxy) gene from snapdragon is developmentally and circadian clock regulated. Plant Physiol. 120: 401-10 da Mota RV, Cordenunsi BR, Nascimento J, Purgatto E, Rosseto M, Lajolo FM (2002) Activity and expression of banana starch phosphorylases during fruit development and ripening. Planta 216: 324-333 Myers AM, Morell MK, James MG, Ball SG (2000) Recent progress toward understanding biosynthesis of the amylopectin crystal. Plant Physiol 122: 989-997 Nakamura Y, Umemoto T, Takahata Y, Komae K, Amano E, Satoh H (1996) Change in the structure of starch and enzyme activities affected by sugary mutations in developing rice endosperm. Possible role of starch debranching enzyme (R-enzyme) in amylopectin biosynthesis. Physiol. Plant. 97: 491-98 Newgard CB, Huang PK, Fletterick RJ (1989) The family of glycogen phosphorylase: structure and function. Crit Rev. Biochem. Mol. Biol. 24: 69-99 Pas HH, Robillard GT (1988) S-phosphocysteine and phosphohistidine are intermediates in the phosphoenopyruvate-dependent mannitol transport catalyzed by Escherichia coli EIIMtl. Biochemistry 27: 5835-5839 Schupp N, Ziegler P (2004) The relation of starch phosphorylases to starch metabolism in wheat. Plant Cell Physiol. 45: 1471-1484 Sikmann A, Meyer H (2001) Phosphoamino acid analysis. Proteomics 1: 200-206 Smith AM, Denyer K, Martin C (1997) The synthesis of starch granule. Annu. Rev. Plant. Physiol. Mol. Biol. 48: 67-87 Smith AM, Zeeman SC, Smith SM (2005) Starch degradation. Annu. Rev. Plant Biol. 56: 73-97 Smith AM, Zeeman SC, Thorneycrofy D, Smith SM (2003) Starch mobilization in leaves. J. Exp. Bot. 54: 577-583. Steup M (1988) Starch degradation. In J. Preiss, ed, The Biochemistry of Plants, Vol 14. Academic Press, San Diego, CA, pp 255-296 Takaha T, Critchley J, Okada S, Smith SM (1998) Normal starch content and composition in tubers of antisence potato plants lacking D-enzyme (4-a-glucanotransferase). Planta 205: 445-451 Takeda Y, Guan H-P, Preiss J (1993) Branching of amylose by the branching isozymes of maize endosperm. Carbohydr. Res. 240: 253-63 Tetlow IJ, Morell MK, Emes MJ (2004a) Recent developments in understanding the regulation of starch metabolism in higher plants. J. Exp. Bot. 55: 2131-2145 Tetlow IJ, Wait R, Lu Z, Akkasaeng R, Bowsher CG, Esposito S, Kosar-Hashemi B, Morell MK, Emes MJ (2004b) Protein phosphorylation in amyloplasts regulates starch branching enzyme activity and protein-protein interactions. Plant Cell 16: 694-708 Thorbjørnsen T, Villand P, Kleczkowski L, Olsen OA (1996) A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare) Biochem. J. 313: 149-54 Tiessen A, Hendriks JHM, Stitt M, Branscheid A, Gibon Y, Farré EM, Geigenberger P (2002) Starch synthesis in potato tuber is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase. Plant Cell 16: 694-708 Van de Wal M, D’Hulst C, Vincken J-P, Buleon A, Visser R, Ball S (1998) Amylose is synthesized in vitro by extension of and cleavage from amylopectin. J. Biol. Chem. 273: 22232-22240 Vriten P, Nakamura T (2000) Wheat granule-bound starch synthase I and II are encoded by separate genes that are expressed in different tissues. Plant Physiol. 122: 255-263 Wang ZY, Zheng FQ, Shen GZ, Gao JP, Snustad DP, Li MG, Zhang JL, Hong MM (1995) The amylose content in rice endosperm is related to the post-translational regulation of the waxy gene. Plant J. 7: 613-622 Wu C, Colleoni C, Myers AM, James MG (2002) Enzymatic properties and regulation of ZPU1, the maize pullulanase-type starch debranching enzyme. Arch. Biochem. Biophys 406: 21-32 Wu J, Ma QN, Lam SK (1994) Identifying substrate motif of protein kinases by random library approach. Biochemistry 33: 14825-14833 Yaffe MB, Smerdon SJ (2004) The use of in vitro peptide-library screens in the analysis of phosphoserine-threonine-binding domain structure and function. Annu Rev. Biophys. Biomol. Struct. 33: 225-44 Zeeman SC, Thorneycroft D, Schupp N, Chapple A, Weck M, Dunstan H, Haldimann, Bechtold N, Smith AM, Smith SM (2004) Plastidial alpha-glucan phosphorylase is not required for starch degradation in arabidopsis leaves but has a role in the tolerance of abiotic stress. Plant Physiol. 135: 849-858 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/38315 | - |
| dc.description.abstract | 磷酸化是常見的蛋白質轉譯後修飾，同時也是訊息傳導中相當重要的一環。相對於動物界肝糖磷解脢 (glycogen phosphorylase, GP) 具有詳細而完整的磷酸化調控系統，植物細胞中相似度極高的澱粉磷解脢 (starch phosphorylase, SP)，卻從未有同樣的發現；直到2004年Tetlow等人才在小麥造粉體中觀察到澱粉磷解脢有被磷酸化修飾的現象 (Tetlow et al, 2004b )。本實驗室楊光華則在甘藷塊根中純化出針對L型澱粉磷解脢的激脢，並命名為澱粉磷解脢激脢 (L-SP kinase, LSK) (楊光華, 2005)。本論文承續楊光華的研究，進一步精製此激脢，並嘗試以二維電泳的方式進行解析，盼能藉以確定其身份；同時更進一步的藉由蛋白質陣列的實驗，嘗試探討此激脢與澱粉磷解脢之間的辨識關係。 | zh_TW |
| dc.description.abstract | Protein phosphorylation is a common post-translational modification after gene expression, and play an important role in signal transduction. In contrast to the well characterized phosphorylation regulation system to glycogen phosphorylase (GP) in animal cells, the regulation has not been reported on starch phosphorylase (SP) in plant cells. Recently, Tetlow and colleagues observed the phosphorylation of SP in the amyloplast of wheat (Tetlow et al, 2004). In our labortory, Young has purified the specific kinase for the L-form starch phosphorylase (LSK) (Young, 2005). In this study, we have tried to purify LSK-S300, and analyze its identity by two-dimensional electrophoresis. Furthermore, the combination of LSK to its substrate L-SP was performed by peptide array experiment to elucidate the site specific binding of these two proteins. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T16:30:14Z (GMT). No. of bitstreams: 1 ntu-94-R92b47217-1.pdf: 1116479 bytes, checksum: 91f0201c836a5754dee21cbda2a4556d (MD5) Previous issue date: 2005 | en |
| dc.description.tableofcontents | 目錄 1
中文摘要 3 ABSTRACT 4 第一章 前言 5 1.1 澱粉簡述 5 1.1.1 澱粉的構造 5 1.1.2 澱粉的生合成 6 1.1.3 澱粉的分解 11 1.2 澱粉磷解脢 14 1.2.1 發現與分類 14 1.2.2澱粉磷解脢的研究 18 1.2.3 可能涉及的生理反應 19 1.3 蛋白質磷酸化 20 1.3.1 磷酸化分類 22 1.3.2 O-phosphate磷酸化與蛋白質調控 22 1.3.3 激脢與受質的辨識 23 1.4 實驗緣起 24 1.4.1. L-SP會被P-Tyr, P-Ser. P-Thr. 抗體辨識 24 1.4.2. LSK的純化 24 1.4.3. 延伸問題 24 第二章 材料與方法 27 2.1 電泳檢定法 27 2.1.1 原態膠體電泳 27 2.1.2. SDS膠體電泳 31 2.1.3. 製備式電泳與電泳溶離 33 2.1.4. 膠體染色法 34 2.1.5. 膠片乾燥法及護貝 37 2.1.6. 蛋白質電泳轉印法 38 2.2 一般分析法 40 2.2.1 蛋白質定量 40 2.2.2 甘藷塊根澱粉磷解酶L-SP活性分析法 41 2.2.3 甘藷澱粉磷解酶激酶活性分析法 42 2.3 管柱色層分析法 43 2.3.1. 管柱色層層析法之基本操作 43 2.3.2. 膠體澎潤法及前處理 45 2.3.3. 膠體過濾法 46 2.3.4. 離子交換法 47 2.3.5. 疏水性層析法 47 2.3.6 磷酸纖維素 (phosphocellulose, cellulose phosphate) 48 2.3.6 Con A Sepharose 49 2.3.7 5’ AMP Sepharose 50 2.4 免疫學方法 51 2.4.1. 酵素免疫染色法 51 2.5. 酵素粗抽取及硫酸銨分劃 53 2.6 甘藷塊根澱粉 L 型磷解酶 (L-SP) 純化法 55 2.7 甘藷塊根澱粉 L 型磷解酶激酶 (LSK) 純化法 56 2.9 膠體內蛋白酶水解 57 2.10 二次元電泳 59 2.10.1蛋白質沉澱與回溶 59 2.10.2 二次元電泳之蛋白質定量方法： 60 2.10.3. 二維電泳分析 61 2.11蛋白質陣列分析 (PEPTIDE ARRAY ANALYSIS) 63 2.11.1 激脢分析 63 第三章 結果與討論 64 3.1. LSK純化 64 3.1.1 LSK 純化流程 64 3.1.2 討論 69 3.2 進一步精製 70 3.2 LSK的二維圖譜 74 3.3 L-SP 的磷酸化辨識區 (PHOSPHO-MOTIF) 79 第四章 結論 86 REFERENCE 87 | |
| dc.language.iso | zh-TW | |
| dc.subject | 甘藷 | zh_TW |
| dc.subject | 澱粉磷解脢 | zh_TW |
| dc.subject | 激脢 | zh_TW |
| dc.subject | kinase | en |
| dc.subject | sweet potato | en |
| dc.subject | starch phosphorylase | en |
| dc.title | 甘藷塊根澱粉磷解脢激脢之生化學檢定 | zh_TW |
| dc.title | Biochemical Analysis of L-form Starch Phosphorylase Kinase from Sweet Potato Root | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 93-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 林耀輝,林棋財,楊健志,陳翰民 | |
| dc.subject.keyword | 澱粉磷解脢,激脢,甘藷, | zh_TW |
| dc.subject.keyword | starch phosphorylase,kinase,sweet potato, | en |
| dc.relation.page | 89 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2005-07-12 | |
| 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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