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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | Shih-Pai Chang | en |
| dc.contributor.author | 張世白 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:11:31Z | - |
| dc.date.available | 2021-07-01T08:11:31Z | - |
| dc.date.issued | 1999 | |
| dc.identifier.citation | 匡麟芸（1999）玉米穀粒β-澱粉?分泌性及賀爾蒙作用之探討。國立台灣大學植物科學研究所碩士論文 吳淑媛（1991）玉米β-澱粉?的純化與定性。國立台灣大學植物科學研究所碩士論文 陳紀樺（1991）玉米α-澱粉?的純化與定性。國立台灣大學植物科學研究所碩士論文 黃秀雯（1993）不同生長時期之玉米澱粉?活性表現之研究。國立台灣大學植物科學研究所碩士論文 盧煌勝（1994）玉米。抽印自雜糧作物各論第四章，台灣區雜糧發展基金會，臺北市 Beck E (1985) The degradation of transitory starch granules in chloroplast. In R Heath and J Preiss, ed, Regulation of Carbon Partition in Photosynthetic Tissue. American Society of Plant Physiologists. Rokville, MD., p27-44 Beck E and Ziegler P (1989) Biosynthesis and degradation of starch in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 40: 95-117 Beers EP and Duke SH (1988) Localization of α-amylase in the apoplast of pea (Pisum sativum L.) stems. Plant Physiol. 87: 799-802 Beers EP and Duke SH (1990) Characterization of α-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings. Plant Physiol. 92: 1154-1163 Bilderback DE (1973) A simple method to differentiate between α-amylase and β-amylase. Plant Physiol. 51: 594-595 Bradford MM (1976) Rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248 Caspar T, Lin TP, Monroe J, Bernhard W, Spilatro S, Preiss J and Somerville C (1989) Altered regulation of β-amylase activity in mutants of Arabidopsis with lesions in starch metabolism. Proc. Natl. Acad. Sci. USA 86: 5830-5833 Chen MH, Liu LF, Chen YR, Wu HK and Yu SM (1994) Expression of α-amylases, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient. Plant J. 6(5): 625-636 Daynard TB and Kannenberg LW (1976) Relationship between length of actual and effective grain filling period and grain yield of corn. Can. J. Plant Sci. 56: 237-242 Dreier W, Schnarrenberger C and Borner T (1995) Light- and stress-dependent enhancement of amylolytic activities in white and green barley leaves: β-amylases are stress-induced proteins. J. Plant Physiol. 145: 342-348 Dunn G (1974) A model for starch breakdown in higher plants. Phytochemistry 13: 1341-1346 Echeverria E and Boyer CD (1986) Localization of starch bio-synthetic and degradative enzymes in maize leaves. Amer. J. Bot. 73(2): 167-171 Fincher GB (1989) Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains. Annu. Rev. Plant Physiol. Plant Mol. Biol. 40: 305-346 Gan S and Amasino RM (1997) Making sense of senescence. Plant Physiol. 113: 313-319 Greenwood CT and Milne EA (1968) Starch degrading and synthesizing enzymes. A discussion of their properties and action pattern. Adv. Carbohydrate Chem. 26: 281-366 Haapala H (1969) Studies on the activity of beta-amylase in the chloroplast of Stellaria media during prolonged illumination. Physiol. Plant. 22: 140-146 Hedeley CL and Stoddart JL (1972) Patterns of protein synthesis in Lolium temulentum L. J. Exp. Bot. 23: 490-501 Heitz T, Geoffroy P, Fritig B and Legrand M (1991) Two apoplastic α-amylases are induced in tobacco by virus infection. Plant Physiol. 97: 651-656 Hurng WP and Kao CH (1993) Loss of starch and increase of α-amylase activity in leaves of flooded tobacco plants. Plant Cell Physiol. 34: 531-534 Hurng WP, Su LY and Kao CH (1986) Senescence of rice leaves. XVI. Regulation by light. Bot. Bull. Acad. Sin. 27: 163-174 Jacobsen JV, Hanson AD and Chandler PC (1986) Water stress enhances expression of an α-amylase gene in barley leaves. Plant Physiol. 80: 350-359 Kainuma K (1988) Structure and chemistry of the starch granule. In J Preiss, ed, The Biochemistry of Plants Vol.14., Academic Press, New York, p141-180 Kakefuda G and Duke SH (1984) Electrophoretic transfer as a technique for the detection and identification of plant amylolytic enzymes in polyacrylamide gel. Plant Physiol. 75: 278-280 Kakefuda G, Duke SH and Hostak MS (1986) Chloroplast and extrachloroplastic starch-degrading enzymes in Pisum sativum. Planta 168: 175-182 Kakefuda G and Preiss J (1997) Partial purification and characterization of a diurnally fluctuating novel endoamylase from Arabidopsis thaliana leaves. Plant Physiol. Biochem. 35(12): 907-913 Kao CH (1988) Hormone regulation and metabolism of rice leaf senescence. In SS Purohit, ed, Hormonal Regulation of Plant Growth & Development IV., Agro. Botanical Publishers, Bikkaner, p223-239 Kao CH (1994) Endogenous polyamine levels and dark-induced senescence of detached corn leaves. Bot. Bull. Acad. Sin. 35: 15-18 Lin TP, Spilatro SR and Preiss J (1988) Subcellular localization and characterization of amylases in Arabidopsis leaf. Plant Physiol. 86: 251-259 Lizotte PA, Henson CA and Duke SH (1990) Purification and characterization of pea epicotyl β-amylase. Plant Physiol. 92: 615-621 Manga VA and Sharma R (1990) Lack of functional interrelationship between β-amylase photoregulation and chloroplast development in mustard (Sinapis alba L.) cotyledons. Plant Cell Physiol. 31(2): 167-172 Merlo L and Passera C (1991) Changes in carbohydrate and enzyme levels during development of leaves of Prunus persica, a sorbitol synthesizing species. Physiol. Plant. 83: 621-626 Mita S, Suzuki-Fujii K, and Nakamura K (1995) Sugar-inducible expression of a gene for β-amylase in Arabidopsis thaliana. Plant physiol. 107: 895-904 Nakamura K, Ohto M, Yoshida N and Nakamura K (1991) Sucrose-induced accumulation of β-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cuttings of sweet potato. Plant Physiol. 96: 902-909 Pongratz P and Beck E (1978) Diurnal oscillation of amylolytic activity in spinach chloroplast. Plant Physiol. 62: 687-689 Prioul JL and Schwebel-Dugu? N (1992) Source-sink manipulation and carbohydrate metabolism in maize. Crop Sci. 32: 751-756 Saeed M and Duke SH (1990) Amylase in pea tissues with reduced chloroplast density and/or function. Plant Physiol. 94: 1813-1819 Sambrook J, Fritsch EF and Maniatis T (1989) Molecular cloning: A Laboratory Manual, Ed 2. Cold Spring Harbor Laboratory Press, New York Schwabe DL (1970) The control of leaf senescence in Kleinia articulata by photoperiod. Ann. Bot. 34: 43-55 Sharma R and Schopfer P (1982) Sequential control of phytochrome mediated synthesis de novo synthesis of β-amylase on the cotyledons of mustard (Sinapis alba L.) seedling. Planta 155: 183-189 Singh I, Nandwal AS, Kuhad MS and Singh N (1998) Biochemical changes occuring during development of leaves emerged at three different stages in pigeonpea. Indian J Plant Physiol. 3(2): 89-93 Singh N, Luthra R and Sangwan RS (1991) Mobilization of starch and essential oil biogenesis during leaf ontogeny of lemongrass (Cymbopogon flexuosus Stapf.). Plant Cell Physiol. 32(6): 803-811 Subbaramaiah K and Sharma R (1985) Affinity chromatography of mustard β-amylase on starch columns. J Biochem. Biophys. Method 10:315-320 Subbaramaiah K and Sharma R (1989) β-amylase from mustard (Sinapis alba L.) cotyledons. Plant Physiol. 89: 860-866 Thomas H and Stoddart JL (1980) Leaf senescence. Annu. Rev. Plant Physiol. 31: 83-111 Turgeon R (1989) The sink-source transition in leaves. Annu. Rev. Plant Physiol. Plant Mol. Biol. 40: 119-138 Umemura T, Perata P, Futsuhara Y and Yamaguchi J (1998) Sugar sensing and α-amylase gene repression in rice embryos. Planta 204: 420-428 Walk GJ and Hope PM (1963) The action of some α-amylase on starch granules. Biochem. J. 86: 452-462 Wang Q, Monroe J and Sjolund RD (1995) Identification and characterization of a phloem-specific β-amylase. Plant Physiol. 109: 743-750 Wang SM and Huang AHC (1987) Biosynthesis of the lipase in the scutellum of maize kernel. J. Biol. Chem. 262: 2270-2274 Wang SM, Lue WL, Wu SY, Huang HW and Chen J (1997) Characterization of a maize β-amylase cDNA clone and its expression during seed germination. Plant Physiol. 113: 403-409 Weber K and Osborne M (1975) Proteins and sodium dodecyl sulfate: molecular weight determination on polyacrylamide gel and related procedure. In H Neurath and RL Hills, eds, The Proteins., Academic Press, New York, p180-225 Wilson LA, Birmingham VA, Moon DP and Snyder HE (1978) Isolation and characterization of starch from mature soybeans. Cereal Chem. 55: 661-670 Wingler A, von Schaewen A, Leegood RC, Lea PJ and Quick WP (1998) Regulation of leaf senescence by cytokinin, sugars, and light. Effects on NADH-dependent hydroxypyruvate reductase. Plant Physiol. 116: 329-335 Yu SM, Kuo YH, Sheu G, Sheu YJ and Liu LF (1991) Metabolic derepression of α-amylase gene expression in suspension-cultured cells of rice. J. Biol. Chem. 266: 21131-21137 Zeeman SC, Northrop F, Smith AM and ap Rees T (1998) A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme. Plant J. 15(3): 357-365 Ziegler P and Beck E (1986) Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplasts. Plant Physiol. 82: 1119-1121 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75037 | - |
| dc.description.abstract | 本論文主要探討玉米葉片之澱粉水解?在老化過程中的變化。分別以整棵植株及初生葉為材料，發現隨著葉齡的增加，會有α-澱粉水解?活性上升及β-澱粉水解?活性下降的現象。利用西方免疫檢定，發現老化過程中β-澱粉水解?活性強度和其蛋白質分子的量成正相關，顯示酵素活性下降的原因是蛋白質的破壞，而不是失活（inactivation）所致。不論是植株葉片之自然老化或葉圓盤之人為老化的試驗結果，都指出α-澱粉水解?活性的上升或β-澱粉水解?活性的下降，皆與一般用做老化指標之可溶性蛋白質含量的變化，呈現高度的相關性；顯示澱粉水解?的活性變化可以做為玉米葉片老化之良好指標，β-澱粉水解?尤其適合。北方或條帶轉印之雜合反應的結果指出，只有在發育中之未完全展開的葉片內才有β-澱粉水解?mRNA的累積，葉片一旦展開之後，其mRNA量即逐漸下降；而當此mRNA下降之時，β-澱粉水解?的活性卻仍因其蛋白質量的增加而提高。葉片切離植物體後，其β-澱粉水解?活性的下降情形不因外加植物荷爾蒙Gibberellin、Zeatin或Abscisic acid而有所改變，但α-澱粉水解?活性則會受到ABA的促進，和蔗糖的抑制；由此推論，在玉米葉片老化過程中，β-澱粉水解?活性下降與α-澱粉水解?活性上升的現象，應是透過不同的調控機制。 | zh_TW |
| dc.description.abstract | Changes of amylase activities in aging maize leaves were studied. The increase in α-amylase activity was accompanied with the decrease in β-amylase activity along the age gradient in a mature plant. Results from immunoblot analyses showed that β-amylase activity was closely correlated with the protein quantity of β-amylase during leaf senescence, and the decrease of β-amylase could be attributed to the protein degradation but not inactivation. No matter whole plant or leaf disc system was studied, leaf total soluble protein showed a highly positive correlation with β-amylase activity, and also a negative correlation with α-amylase activity during senescence. Therefore, changes in α- and β-amylase activities should be able to play a good index for leaf senescence just as total soluble protein content has been used. Based on RNA slot analysis, β-amylase mRNA was synthesized and accumulated when leaf expansion was in progress. Once the leaf reached full expansion, the β-amylase mRNA gradually decreased while the enzyme activity was still increasing owing to the protein synthesis and accumulation. In leaf disc system, the decrease of β-amylase activity during senescence could not be altered by adding phytohormones such as gibberellic acid, zeatin and abscisic acid. And α-amylase activity in leaf discs was enhanced by abscisic acid and repressed by sucrose. These results suggested that regulation of increasing α-amylase and decreasing β-amylase in senescing maize leaf might not share a common mechanism. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:11:31Z (GMT). No. of bitstreams: 0 Previous issue date: 1999 | en |
| dc.description.tableofcontents | 中文摘要……………………………………………………i 英文摘要……………………………………………………ii 前言……………………………………………………1 材料與方法……………………………………………………6 結果……………………………………………………16 一、成熟葉片中之β-澱粉水解?……………………………………………………16 二、初生葉中之β-澱粉水解?……………………………………………………18 三、年輕植株葉片中的β-澱粉水解?……………………………………………………19 四、葉片之人工老化與澱粉水解?的變化……………………………………………………21 五、荷爾蒙及醣類對於葉片老化過程中澱粉水解?活性的影響……………………………………………………22 討論……………………………………………………24 參考文獻……………………………………………………30 圖表……………………………………………………37 | |
| dc.language.iso | zh-TW | |
| dc.title | β-澱粉水解?在玉米葉片老化過程之表現 | zh_TW |
| dc.title | Expression of β-Amylase in Senescing Maize Leaf | en |
| dc.date.schoolyear | 87-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 36 | |
| 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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