請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76214完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | Ming-Chuan Wang | en |
| dc.contributor.author | 王銘川 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:19:11Z | - |
| dc.date.available | 2021-07-01T08:19:11Z | - |
| dc.date.issued | 1996 | |
| dc.identifier.citation | 張奕元（1995）絲瓜果實韌皮部蛋白質的純化、鑑定與定位。國立台灣大學植物研究所碩士論文 莊榮輝（1985）水稻蔗糖合成?之研究。國立台灣大學農業化學研究所博士論文 Aitken, A., Geisow, M., Findlay, J.B., Holmes, C., Yarwood, A. (1989) Peptide preparation and characterization. In: Protein sequencing -a practical approach. Findlay, J.B.C. and Geisow, M.J. (eds). IRL press, Oxford England, pp. 43-68 Allen, A.K. (1979) A lectin from the exudate of the fruit of the vegetable marrow (Cucurbita pepo) that has specificity for β-1,4-linked N-acetylglucosamine oligosaccharides. Biochem. J. 183: 133-137 Alosi, M.C., Melroy, D.L., Park, R.B. (1988) The regulation of phloem exudate from Cucurbita fruit by dilution, glutathione and glutathione reductase. Plant Physiol. 86: 1089-1094 Baba, K., Ogawa, M., Nagano, A., Kuroda, H., Sumiya, K. (1991) Developmental changes in the bark lectin of Sophora japonica L. Planta 183:462-470 Behnke, H.D, Sjolund, R.D. (1990) Sieve Elements: Comparative Structure, Induction and Development. Springer-Verlag, Berlin. pp. 266-283 Behnke, H.D., Kiritsis, U. (1983) Ultrastructure and differentiation of sieve elements in primitive angiosperms. I. Winteraceae. Protoplasma 118: 148-156 Bentwood, B. J., Cronshaw, J. (1978) Cytochemical localization of adenosine triphosphatase in the phloem of Pisum sativum and its relation to the function of transfer cells. Planta 140: 111-120 Bentwood, B.J, Cronshaw, J. (1976) Biochemistry and cytochemical localization of acid phosphatase in the phloem of Nicotiana tabacum. Planta 130: 97-104 Beyenbach, J, Weber, C, Kleinig, H. (1974) Sieve tube proteins from Cucurbita maxima. Planta 119: 113-124 Bostwick, D.E., Dannenhoffer, J.M., Skaggs, M.R., Larkins, B.A., Thompson, G.A. (1992) Pumpkin phloem lectin genes are specifically expressed in companion cells. Plant Cell 4: 1539-1548 Bostwick, D.E., Skaggs, M.I., Thompson, G.A. (1994) Organization and characterization of Cucurbita phloem lectin genes. Plant Mol. Biol. 26: 887-897 Bostwick, D.E., Thompson, G.A., (1993) Nucleotide sequence of a pumpkin phloem lectin cDNA. Plant Physiol. 102: 693-694 Bouck, G.B., Cronshaw, J. (1965) The fine structure of differentiating sieve tube elements. J. Cell Biol. 95: 79-96 Bradford, M.M. (1976) Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254 Bumette, W.H., (1981) Western Blotting: electrophoretic transfer of proteins from SDS-polyacrylamide gel to unmodified nitrocellulose and radiographic detection with antibody and radioiodionated protein A. Anal. biochem. 112:195-203 Carrey, E.A. (1989) Peptide mapping. In: Protein Structure-A Practical Approach. Creighton, T.E. (eds). IRL Press, Oxford England, pp.117-153 Catesson, A.M. (1973) Observations cytochimiques sur les tubes cri de quelques angiospermes. J. Microsc. Paris 16:95-104 Clausen, S., Apel, K. (1991) Seasonal changes in the concentration of major storage protein and its mRNA in xylem ray cell of poplar trees. Plant Mol. Biol. 17:669-678 Coleman, G.D., Chen, T.H.H., Ernst, S.G., Fuchigami, L. (1991) Photoperiod control of bark storage protein accumulation. Plant Physiol 96: 686-692 Cronshaw, J. (1975a) P-proteins. In: Aronoff S, Dainty J, Gorham P.R., Srivastava L.M., Swanson C.A. (eds) Phloem Transport. Plenum, New York London, Paris, pp 429-430 Cronshaw, J. (1975b) Sieve Element Walls. In Aronoff, S., Dainty, J., Gorham, P.R., Srivastava, L.M., Swanson, C.A. (eds) Pholem transport. Plenum, New york London pp. 129-147 Cronshaw, J. (1981) Phloem structure and function. Annu. Rev. Plant Physiol. 32:465-482 Cronshaw, J. (1985) The fine structure of phloem cells. In: Proc 43rd Annu Meet Electron Microscopical Society of America. San Francisco Press, San Francisco, pp. 632-635 Cronshaw, J. (1986 a) P-protein in the phloem of Cucurbita I. The development of P-protein bodies. J. Cell Biol. 38:25-39 Cronshaw, J. (1986 b) P-protein in the phloem of Cucurbita II. The p-protein of mature sieve element. J. Cell Biol. 38-292-303 Cronshaw, J., Anderson, R. (1971) Phloem differentiation in tabacco pith culture. J. Ultrastruct Res. 34:244-259 Cronshaw, J., Esau, K. (1967) Tubular and fibrillar components of mature and differentiating sieve elements. J. Cell. Biol. 34: 801-816 Cronshaw, J., Gilder, J., Stone, D. (1973) Fine structural studies of P-protein in Cucurbita, Cucumis and Nicotiana. J. Ultrastruct. Res. 45: 192-205 Cronshaw, J., Sabnis, D.D. (1990) Phloem protein. In: Behnke, H.D., Sjolund, R.D. (eds) Sieve element. Springer-verlag Berlin press. pp. 266-283 Dickmann, D.I., Kozolowiski, T.T. (1968) Mobilization by Pinus resinosa cones and shoots of 14C photosynthate from needles of different ages Amer. J. Bot. 55: 990-996 Easu, K. (1969) The phloem. In: Zimmermann, W., Ozenda, P., Wulff, H.D. (eds) Encyclopedia of Plant Anatomy, Berlin Stuttgart, 505p. Easu, K., Cheadle, V.I. (1965) Cytological studies on phloem. Univ. Cal. Publ. Bot. 36: 253-344 Eichorn, S.E. (1974) Sieve element ultrastructure in platycerium bifuracatum and some other polypodiaceous ferns: the nucleus. Planta 119:301-318 Esau, K (1978) The protein inclusions in sieve elements of cotton (Gossypium hirsutum L.). J. Ultrastruct. Res. 63: 224-235 Esau, K., Charvat, I.D (1975) An ultrastructural study of acid phosphatase localization in cells of Pllaseolus vulgaris phloem by the use of the azo-dye method. Tissue Cell 7: 619-630 Esau, K., Cronshaw, J. (1967) Tubular components in cells of healthy and tobacco mosaic virus-infected Nicotiana. Virology 33: 26-35 Eschrich, W., Evert, R.F., Heyser, W. (1971) Proteins fo sieve tube exudate of Cucurbita maxima. Planta 100: 208-221 Freundlich, A. (1974) No polysaccharide demonstrated in filamentous structures in sieve elements by Thiery's periodic acid-thiocarbohydrazide-silver protein method for electron microscopy. Planta 118: 85-87 Gaffney, T., Friendrich, L., Vernooij, B., Negrotto, D., Nye, G., Uknes, S., Ward E., Kessmann, H., Ryals, J. (1993) Requirement of salicylic acid for the induction of systemic acquired resistance. Science 261:754-756 Garvey, J.S., Cremer, N.E., Susdorf, D. H. (1977) Methods in Immunology: A Laboratory Text for Instruction and Research, W.A. Benjamin, Northampton, Mass Gietl, C., Kauss, H., Ziegler, H. (1979) Affinity chromatography of a lectin from Robinia pseudoacacia L. and demonstration of lectins in sieve tube sap from other tree species. Planta 144: 367-372 Gilder, J., Cronshaw, J. (1973a) The distribution of adenosine triphosphatase activity in differentiating and mature phloem cells of Nicotiana tabacum and its relationship to phloem transport. J. Ultrastruct. Res. 44: 388-404 Gilder, J., Cronshaw, J. (1973b) Adenosine triphosphatase in the phloem of Cucurhita. Planta 110: 189-204. Gilder, J., Cronshaw, J. (1974) A biochemical and cytochemical study of adenosine triphosphatase activity in the phloem of Nicotiana tabacum. J. Cell Biol. 60: 221-235 Hall, S.M., Baker, D.A. (1972) The chemical composition of Ricinus phloem exudate. Planta 106: 131-140 Hancock, W.S. (1984) Handlebook of HPLC for the Separation of Amino acids, Peptides, and Proteins, Vol. I. CRC Press, Boca Raton, FL. Heinrikson, R. L., Meredith, S. C. (1984) Amino acid analysis by reversed-phased high-performance liqiud chromatography: Precolumn Derivatization with phenylisothiocyanate. Ana. Bioch. 136: 65-74 Hider, V.A., Gatehouse, A.M.R., Boulter, D. (1993) Transgenic plants conferring insect tolerance: protease inhibitor approach. In: Transgenic Plants vol I. Engineering and Utilization. Kung S, and Wu R. (eds.) Acadmic. Press, pp. 317-338 Hill, D. W., Walters, F. H., Wilson, T.D., Stuart, J.D. (1979) High performance liquid chromatographic determination of amino acid in the picomole range. Ana. Chem. 55: 1338-1341 Hooley, R. (1984) Gibberellic acid controls the secretion of acid phosphatase in aleurone layers and isolated aleurone protoplasts of Avena fatua. J. Exp. Bot. 35: 822-828 Hughes, G.T., Wilson, K.J. (1983) High-performance liquid chromatography: Analytical and preparative applications in protein structure determination. Meth. Biochem. Anal. 29: 59-135 Hunkapiller, M.W., and Lujan, E., Ostrandander, F., Hood, L.E. (1983) Purification of microgram quantities of protein from polyacrylamide gel for amino acid sequence analysis. Meth. Enzymol. 91: 227-236. Ilker, R.E., Currier, H.B., (1974) Heavy meromyosin complexing filaments in the phloem of Vicia faba and Xylosma congestum. Planta 120: 311-316 Ilker, R.E., Curner, H.B. (1975) Histochemical studies of an inclusion body and P-protein in phloem of Xylosma congestum. Protoplasma 85: 127-132 Ishiwatari, Y., Honda, C., Nakamura, S., Hirano, H., Mori, S., Fujiwara, T., Hayashi, H., Chino, M. (1995) Thioredoxin h is one the major protein in rice phloem sap. Planta 195: 456-463 Kauss, H., Ziegler, H. (1974) Carbohydrate-binding proteins from the sieve-tube sap of Robinia pseudoacacia. Planta 121: 197-200 Kennecke, M., Ziegler, H., de Fekete, M.A.R. (1971) Enzyme activities in the sieve sap of Robinia pseudoacacia L. and of other tree species. Planta 98: 330-356 Kleinig, H., Dorr, I., Kollmann, R. (1971a) Vineblastine-induced precipitation of phloem proteins in vitro. Protoplasma 73: 993-302 Kleinig, H., Dorr, I., Weber, C., Kollmann, R. (1971 b) Filamentous protein from plant sieve tubes. Nature New Biol. 229: 152-153 Kleinig, H., Thoenes, J., Dorr, I. Kollmann, R. (1975) Filament formation in vitro of a sieve tube protein from Cucurbita maxima and Cucurbita pepo. Planta 127: 163-170 Kollmann, R. (1980) Fine structural and biochemical characterization of phloem proteins. Can J Bot 58: 802-806 Laemmi, U.K. (1970) Cleavage of protein during the assembly of the head of bacteriophage T4. Nature 227: 680-685 Lawton, D.M. (1978) P-protein crystals do not disperse in uninjured sieve elements in roots of runner bean (Phaseolus multiflorus) fixed with glutaraldehyde. Ann. Bot. 42: 353-361 Lehmann, J. (1973) Studies on the phloem exudate of Cucurbita pepo L. Planta 114: 51-61 McEuen, A.R., Har, t J.W., Sabnis, D.D. (1981) Calcium-binding protein in sieve tube exudate. Planta 151: 531-534 Murmanis, L., Evert, R.F. (1996) Some aspects of sieve cell ultrastrusture in Pinus Strobus. Amer. J. Bot. 53: 1065-1078. Murrary, C., Christeller, J.T. (1995) Purification of a trypsin inhibitor from Pumpkin fruit phloem exudate and isolation of Putativetrypsin and chymotrypsin inhibitor cDNA clones. Bio. Chem. Hoppe-Seyler 376: 281-287 Nakamura, S., Hayashi, H., Mori, S. (1993) Protein phosphorylation in the sieve tubes of rice plants. Plant Cell Physiol. 34: 927-933 Newcomb, E.H. (1967) A spiny vesicle in the slime-producing cells of the bean root. J. Cell. Biol. 35: 17-22 Nuske, J., Eschrich, W. (1976) Synthesis of P-protein in mature phloem of Cucurbita maxima. Planta 132: 109-118 O'Farrel, P.H. (1975) High-resolution two-dimensional electrophoresis of protein. J. Biol. Chem. 250: 4007-4021 Palevitz, B.A., Newcomb, E.H. (1971) The ultrastructure and development of tubular and crystalline P-protein in the sieve elements of certain papilionaceous legumes. Protoplasma 72: 399-426 Read, S.M., Northcote, D.H. (1983) Subunit structure and interaction of phloem protein of Cucurbita maxima (Pumpkin). Eur. J. Biochem. 134: 561-569 Read, S.M., Northcote, D.H. (1983b) Subunit structure and interactions of the phloem proteins of Cucurbita maxima (pumpkin). Eur. J. Biochem. 134: 561-569 Read, S.M., Northcote, D.H. (1983a) Chemical and immunological similarities between the phloem proteins of three genera of the Cucurbitaceae. Planta 158: 119-127 Sabnis, D.D., Hart, J.W. (1976) A comparative analysis of phloem exudate proteins from Cucumis melo, Cucumis sativus and Cucurbita maxima by polyacrylamide gel electrophoresis and isoelectric focussing. Planta 130: 211-218 Sabnis, D.D., Hart, J.W. (1978) The isolation and some properties of a lectin (hameagglutinin) from Cucurbita phloem exudate. Planta 142: 97-101 Sabnis, D.D., Hart, J.W. (1979) Heterogeneity in phloem protein complements from different species. Consequences to hypotheses concerned with P-protein function. Planta 145: 459-466 Sabnis, D.D., Hart, J.W. (1974) Studies on the possible occurrence of actomyosin-like protein in phloem. Planta 118: 271-281 Salinovich, O., Motelaro, R. (1986) Reversible staining and peptide mapping of proteins transferred to nitrocellulose after separation by SDS-PAGE. Anal. Biochem. 156: 341-347 Schulz, A.S., Alosi, A.C., Sabnis, D.D., Park, R.B. (1989) A phloem-specific, lectin-like protein is located in pine sieve-element plastids by immunocytochemistry. Planta 119: 506-515 Sham, M.H., Northcote, D.H. (1987) Transcription and translation of phloem protein (PP2) during phloem differentiation in Cucurbita maxima. Planta 170: 392-399 Sloun, R.T., Sabnis, D.D., Hart, J.N. (1976) The heterogeneity of phloem exudate from different plants: A comparative survey often plants using polyacrylamide gel electrophoresis. Planta 133: 97-102 Smith, L.M., Sabnis, D.D., Johnson, R.P.C. (1987) Immunocytochemical localization of phloem lectin from Cucurbita maxima using peroxidase and colloidal gold labels. Planta 170: 461-470 Stone, D.L., Cronshaw, J. (1973) Fine structure of P-protein filaments from Ricinus communis. Planta 113: 193-206 Toth, K.F., Wang, Q., Sjolund, R.D. (1994) Monoclonal antibodies against phloem p-protein from plant tissue cultures. I. Microscopy and biochemical analysis. Amer. J. Bot. 81: 1370-1377 Tuzun, S., Rao, M.N., Vogeli, U., Schardl, C. L., Kuc, J. C. (1989) Induced systemic resistance to blue mold: Early induction and accumulation of b-1-3-glucanasses, chintinases, and other pathogensis-related protein (b-proteins) immunized tabacco. Phytopathology 79: 979-983. Varndell, I.M., Polark, J.M. (1986) Electron microscopical immunocytochemistry. In: Immunocytochemistry - Modern Method and Application. Polak J.M., Noorden S.V. (eds) Wright Press. Britain. pp. 146-166. Volkin, V. B., Keibanov, A.M. (1989) Minimizing protein inactivation. In: Protein function - a practical approach. Creighton T. E. (eds). IRL Press, Oxford England, pp. 1-24 Wang, M.B., Boulter, D., Gatehouse, J.A. (1994) Characterization and sequencing of cDNA clone encoding the phloem protein PP2 of Cucurbita pepo. Plant Mol. Biol. 24: 159-170 Wang, Q., Monroe, J., Sjolund, R.D. (1995) Identification and characterization of phloem-specific β-amylase. Plant Physiol. 109:743-750 Ward, E.R., Uknes, S.J., William, S.C., Dincher, S.S., Wederhold, D.L. Ahl--Goy, P., Metraux, J.P., Ryals, J.A. (1991) Coordinate gene activity that induced systemic acquired resistance. Plant Cell 3: 1085-1094 Weber, C., Kleinig, H. (1971) Molecular weights of Cucurbita sieve tube proteins. Planta 99: 179-182 Wergin, W.P., Newcomb, E.H. (1970) Formation and dispersal of crystalline P-protein in sieve elements of soybean (Glycine max L.). Protoplasma 71: 365-388 Weter, C., Franke, W.W., Kartenbeck, J. (1974) Structure and biochemistry of phloem-proteins from Cuccurbita maxima. Exp. Cell Res. 87: 79-106 Williamson, R.E., (1979) An investigation of the contractile protein hypothesis of phloem translocation. Planta 106: 149-157 Woloshuk, C.P., Meulenhoff, J.S., Sela-Burrlage, M., Eizen, V.D., Cornelissen, B.J.C. (1991) Pathogen-induced protein with inhibitory activity toward Phytophtora infestans. Plant Cell. 3: 619-628 Woodin, F.B.P. (1969) P-protein and microtubular systems in Nicotiana callus phloem. Planta 85: 284-98 Yalpani, N., Alexander, J.E., Jose, L., Ilya, R. (1994) Ultraviolet and ozone stimulate accumulation for salicylic acid pathogenesis-related proteins and virus resistance in tabacco. Planta 193: 372-376 Yapa, P.A.J., Spanner, D.C. (1972) The effect of protease digestion (in situ) on the slime substance of mature sieve tubes. Planta 107: 89-96 Yarwood, A. (1989) Manual methods of protein sequence. In: Protein Sequencing - A Practical Approach. Findlay, J.B.C., Geisow, M.J. (eds). IRL Press, Oxford England, pp. 119-145 Yoshida, k., Baba, K., Yamamoto, N., Tazaki, K. (1994) Cloning of a lectin cDNA and seasonal changes in leaves of the lectin and its mRNA in the inner bark of Robinia pesudoaceae. Plant Mol. Biol. 25: 845-853 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76214 | - |
| dc.description.abstract | 在七美絲瓜（Luffa cylindrica Var. Seven Beauty）韌皮部溢流物中，經原態電泳分析蛋白質分子量分佈極廣，且有明顯10群主要蛋白質。利用修飾的雙向電泳進行占28.2％的85 kDa蛋白質純化。此主要蛋白質帶在第二方向變性膠體出現48、42.5、32、28、25蛋白質帶，其中以42.5 kDa為最主要蛋白質並且給予回收，回收率達15.98％。回收蛋白質經HPLC Reverse-phase Column分析在3.81分鐘的延遲時間22.86％的acetonitrile被沖洗為單一純化蛋白質。在西方墨漬法證實兩者免疫親緣關係，42.5kDa為85kDa蛋白質的次體。在42.5kDa蛋白質氨基酸成分以Glycine，Histidine為主要氨基酸共佔39.61％。另外，在經溴化氰斷裂後產生39.47、34.8、28.3、21.91、20.68kDa勝?片段，其中39.47kDa勝?的氨基端氨基酸序列為DTHFHVAVTTWTTK。28.3kDa勝?的氨基端氨基酸序列為TTGGDGGLGTKG。 在免疫螢光及免疫電顯定位下，85 kDa蛋白質只發現專一性分佈在維管束中老化的篩胞及導管細胞中。因此可知，在韌皮部溢流物的85kDa蛋白質為維管束專一性之晚期表現的蛋白質。 | zh_TW |
| dc.description.abstract | Phloem exudate obtained from Luffa cylindrica var. Seven Beauty fruit was separated with modified 2-D gel electrophoresis. A major protein of 85 kDa occupying about 28.2% of total proteins had 5 bands on denatured gel. One of major proteins at 42.5 kDa was further identified by Reversed - Phase HPLC showing one peak on 3.81 minute retention time and 22.86% acetonitrile. The cross reaction of the western blotting occurred on both 85 kDa and 42.5 kDa proteins, and it implied that 42.5 kDa was a subunit of 85 kDa protein. Glycine and Histidine that occupied 39.61% of total amino acid were major amino acid component of 42.5 kDa protein. The 42.5 kDa protein was digested into 20.68, 21.91, 31.96, 34.28 and 39.47 kDa peptide fragments by cyanogen bromide. The N-terminal amino acid sequence of 39.47 kDa is DTHFHVAVTTWTTK and 31.96 kDa is TTGGDGGLGTKG. Immunocytochemistry showed that 85 kDa protein only presented mature sieve element and vessel. It indicated that 85 kDa protein is specific for later expression in vascular bundle. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:19:11Z (GMT). No. of bitstreams: 0 Previous issue date: 1996 | en |
| dc.description.tableofcontents | 一、前言……………………………………………………1 前人研究……………………………………………………2 二、材料與方法……………………………………………………9 （一）研究材料……………………………………………………9 （二）絲瓜果實韌皮部溢流物的收集……………………………………………………9 （三）絲瓜果實韌皮部溢流物中蛋白質的純化……………………………………………………9 （四）抗體製備……………………………………………………24 （五）免疫螢光組織定位……………………………………………………28 （六）免疫膠體金次細胞定位……………………………………………………29 三、結果……………………………………………………32 （一）絲瓜各部分含蛋白質量……………………………………………………32 （二）七美絲瓜果實韌皮部溢流雙向電泳分析……………………………………………………34 （三）胺基酸水解分析……………………………………………………46 （四）蛋白質斷裂……………………………………………………47 （五）抗體製備……………………………………………………49 （六）抗體專一性測試……………………………………………………50 （七）組織定位……………………………………………………54 （八）免疫電子顯微鏡標定……………………………………………………58 四、討論……………………………………………………61 未來可繼續研究方向……………………………………………………67 五、參考文獻……………………………………………………68 | |
| dc.language.iso | zh-TW | |
| dc.title | 七美絲瓜果實溢流42.5kDa蛋白質純化、鑑定與免疫定位 | zh_TW |
| dc.title | Purification, Identification and Immunolabling of a 42.5kDa Protein Obtained from Fruit Phloem Exudat of Luffa cylindrica | en |
| dc.date.schoolyear | 84-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 75 | |
| 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 | |
文件中的檔案：
沒有與此文件相關的檔案。
系統中的文件，除了特別指名其著作權條款之外，均受到著作權保護，並且保留所有的權利。