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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | 靳宗洛 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:14:11Z | - |
| dc.date.available | 2021-07-01T08:14:11Z | - |
| dc.date.issued | 1987 | |
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ED Clman, L Schoffl, JL Key 1984 Comparative analysis of physical stress response in soybean seedling using cloned heat shock cDNA. Plant Mol. Biol. 3: 45-58 10. Dawson WO, GL Grantham 1981 Inhibition of stable RNA synthesis and production of a novel RNA in heat shock stressed plants. Biochem. Biophy. Res. Commun. 100: 23-30 11. Ericson MC, SH Alfinito 1984 Proteins produced during salt stress in tobacco cell culture. Plant Physiol. 74: 506-509 12. Gerner EW, MJ Schneider 1975 Induced thermal resistance in HeLa cells. Nature 256: 500-503 13. Heikkila JJ, JET Papp, GA Schultz, JD Bewlwy 1984 Induction of heat shock protein messenger RNA in maize mesocotyls by water stress, abscisic acid and wounding. Plant Physiol. 76: 207-274 14. Hidetoshi J, I Yakara 1984 Durable synthesis of high molecular weight heat shock proteins in G∞ cell of yeast and other eucaryotes. J. Cell Biol. 99: 199-207 15. Hsiao TC 1970 Rapid changes in levels of polyribosomes in Zea Mays in response to water stress. 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McAlister L, DB Finkelstein 1980 Heat shock proteins and thermal resistance in yeast. Biochem. Biophys. Res. Commun. 93: 819-824 36. Miassod R, C Got 1984 An immumnological approach to quantitate RNA polymerase in plant cell extract. Planta 162: 427-433 37. Minton KW, P Karmin, GM Hahn, AP Minton 1982 Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins. Proc. Natl. Acad. Sci. USA 79: 7107-7111 38. Mitchell HK, G Moller, NS Peterson, L Lipps-Sarmiento 1979 Specific protection from phenocopy induction by heat shock. Dev. Genet 1: 181-192 39. Morilla CA, JS Boyer, RH Hageman 1973 Nitrate reductase activity and polyribosome content of corn (Zea Mays L.) having low leaf water potentials. Plant Physiol. 51: 817-824 40. Neidhardt FC, RA Van Bogelen 1981 Positive regulatory gene for temperature-controlled proteins in Escherichio coli. Biochem. Biophys. Res. Commun. 100: 894-900 41. Neidhardt FC, RA Van Bogelen, V Vaughan 1984 The genetics and regulation of heat shock proteins. Annu. Rev. Genet. 18: 295-329 42. Peterson NS, HK Mitchell 1981 Recovery of protein synthesis after heat shock: prior heat-treatment affects the ability of cells to translated mRNA. Proc. Acad. Sci. USA 78: 1708-1711 43. Ritossa F 1962 A new puffing pattern induced by temperature shock and DEP in Drosophila. Experientia 18: 571-573. 44. Sachs MM, TH HO 1986 Alternation of gene expression during environmental stress in plants. Annu. Rev. Physiol. 37: 363-376 45. Schlesinger MJ, G Aliperti, PM Kelley 1982 B. The response of cells to heat shock. Trends in Biochem. Sci. 6: 222-225 46. Schlesinger MJ, M Ashburner, A Tissieres 1982 A Heat shock: from Bacteria to Man. Cold Spring Harbour Laboratory, New York 47. Schlesigner MJ 1986 Heat shock proteins: the search for functions. J. Cell Biol. 103: 321-325 48. Storti RV, MP Scott, A Rich, ML Pardue 1980 Translational control of protein synthesis in response to heat shock in Drosophila melanogaster cells. Cell 22: 825-834 49. Tilly K, N Mckittrick, M Zylicz, C Geogopoules 1983 The dnak protein modulates the heat-shock response of Escherichia coli. Cell 34: 641-646 50. Tisseres A, HK Mitchell, U Tracy 1974 Protein synthesis in salivary glads of Drosphila melanogaster: Relation to chromosome puffs. J. Mol. Biol. 84: 389-398 51. Velasquez J, BD Didomenico, S Lindquist 1980 Intracellular localization of heat shock proteins in Drosophila. Cell 20: 679-689 52. Velazquez J, S. Lindquist 1984 HSP 70: Nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell. 36: 655-662 53. Velazquez J, S Sonoda, GE Bugaisky, S Lindquist 1983 Are HS proteins present in cells that have no been heat shocked J. Cell Biol. 96: 286 54. Wu MT, SJ Wallner 1983 Heat stress response in cultural plant cells. Plant Physiol. 72: 817-820 55. Yamanori T, T Yura 1982 Genetic control of heat shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 79: 860-864 56.林蔚靖,1982,國立台灣大學植物科學研究所碩士論文 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75613 | - |
| dc.description.abstract | 以生長四十小時後的大豆黃化(etiolated)幼苗為材料,用 3H -白胺酸標誌蛋白質,經高速離心後取去核糖體上清液,以硫酸銨分劃,發現所有的熱休克蛋白質均集濃在70?100%硫酸銨分劃區中。以此分劃區來研究蛋白質的生理功能,可得以下結論:首先,對於熱休克蛋白質本身而言,除了在熱休克過程中對於熱反應具穩定性外,更有保護它種蛋白質在熱休克下不被變性的能力。這種保護效果與所加入熱休克蛋白質的量成正比,同時其所保護的對象則傾向於與膜系統相結合的蛋白質。這些熱休克蛋白質不論是在活體內或試管中均表現出對於熱反應具有穩定性。幼苗合成出熱休克蛋白質後,重新置?正常生長溫度,觀察熱休克蛋白質被保留程度,經四天後發現熱休克蛋白質依然存在。同時也認為在所有的熱休克蛋白質族群中,以15?18KD這群低分子量的熱休克蛋白質,在提供植物獲得熱保護的過程中所做的貢獻遠超過高分子量的熱休克蛋白質。 前人對於熱休克蛋白質的研究,均以其次單位(subunit)為對象,至於這些蛋白質在活體內的可能真正結構(native form),至今仍然沒有任何文獻可供參考。在本論文中,藉由膠體過濾法及離子交換法,在熱休克蛋白質純化過程中,可觀察這些次單位在活體中的可能結合形式。其中以15?18KD會與22KD及70KD等相互地結合在一起,68?92KD這群高分子量則可能結合成為一個群體,至於27KD這群,則不參雜其他次單位,而獨自存在。 | zh_TW |
| dc.description.abstract | All the heat shock (HS) proteins from a postribosomal supernatant of heat shocked soybean seedlings were found to be enriched in a 70-100% (NH4)2SO4 fraction. This HS protein enriched fraction was quite resistant to heat denaturation. Moreover, this fraction, when added to the postribosomal supernatant from control (non-heat shocked) seedlings, showed a significant ability to protect proteins from heat denaturation. Heated at 55℃, some 50% of the control proteins, which were normally denatured after HS treatment, were protected for at least 1 hr when 1 mg of this HS protein fraction was added. The degree of protection was proportional to the amount of HS protein fraction added. What's more, these HS proteins have a tendency to protect membrane system binding proteins. Low molecular weight (LMW) 15-18 kD HS proteins contribute more than high molecular weight (HMW) 68-92 kD varieties to plants in terms of providing thermaltolerance. Gel filtration and ion exchanger chromatography were effective in purification of HS proteins. The native form of HS proteins in vivo were also detected. Such subunits as 15-18kD, 22kD and 70kD HS proteins would associate together as a unit. HMW ranging from 68-92 kD HS proteins would form another one. As for 27kD HS proteins, they would not contaminate with other submits. They exist by themselves. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:14:11Z (GMT). No. of bitstreams: 0 Previous issue date: 1987 | en |
| dc.description.tableofcontents | 英文摘要………………………1 中文摘要………………………3 緒言………………………5 實驗材料與方法………………………11 結果………………………20 討論………………………30 參考文獻………………………72 | |
| dc.language.iso | zh-TW | |
| dc.title | 熱休克蛋白質的純化及其生理功能 | zh_TW |
| dc.title | Purification of Heat Shock proteins and their Physiological Functions | en |
| dc.date.schoolyear | 75-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 81 | |
| 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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