請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43508完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 莊榮輝(Rong-Huay Juang) | |
| dc.contributor.author | Yu-Ting Sui | en |
| dc.contributor.author | 眭毓庭 | zh_TW |
| dc.date.accessioned | 2021-06-15T02:22:36Z | - |
| dc.date.available | 2012-08-20 | |
| dc.date.copyright | 2009-08-20 | |
| dc.date.issued | 2009 | |
| dc.date.submitted | 2009-08-19 | |
| dc.identifier.citation | 吳裕仁 (1994) 酵母菌中鎘結合蛋白質的純化與性質分析。碩士論文。國立台灣大學農業化學所，台北。
林士民 (1998) 裂殖性酵母菌對重金屬鎘之隔離與排除機制。博士論文。國立台灣大學農業化學所，台北。 吳建興 (2000) 裂殖性酵母菌中植物螯合素合成酶的分離與性質分析。博士論文。國立台灣大學農業化學所，台北。 簡虹琪 (2001) 布袋蓮中植物螯合素的純化與性質分析。碩士論文。國立台灣大學農業化學所，台北。 邱創儉 (2001) 裂殖性酵母菌中植物螯合素合成 何子潔 (2002) 重金屬鎘在布袋蓮中的隔離與輸送之研究。碩士論文。國立台灣大學農業化學所，台北。 Beck A, Lendzian K, Oven M, Christmann A, Grill E (2003) Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates. Phytochemistry 62:423-431 Bernhard WR, Kagi JH (1987) Purification and characterization of atypical cadmium-binding polypeptides from Zea mays. Experientia Suppl 52: 309-315 Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254 Cherian MG, Apostolova MD (2000) Nuclear localization of metallothionein during cell proliferation and differentiation. Cell Mol Biol 46(2): 347-356 Chen J, Zhou J, Goldsbrough PB (1997) Characterization of phytochelatin synthase from tomato. Physiol Plant 101: 165-172 Clemens S, Kim EJ, Neumann D, Schroeder JI (1999) Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast. EMBO J 18: 3325-3333 Clemens S (2005) Evolution and function of phytochelatin synthases. J Plant Physiol 163: 319-332 Cobbett CS (2000) Phytochelatins and their roles in heavy metal detoxification. Plant Physiol 123: 825-832 Delhaize E, Ryan PR, Randall PJ (1993) Aluminum tolerance in wheat (Triticum aestivum L.). II. Aluminum-stimulated excretion of malic acid from root apices. Plant Physiol 103: 695-702 Dameron CT, Smith BR, Winge DR (1989) Glutathione-coated cadmium-sulfide crystallites in Candida glabrata. J Biol Chem 264: 17355-17360 Do-Young Kim, Lucien Bovet, Sergei Kushnir, Eun Woon Noh, Enrico Martinoia and Youngsook Lee (2006) AtATM3 is involved in heavy metal resistance in arabidopsis. Plant Physiol 140: 922-932 Ellman G, Lysko H (1979) A precise method for the determination of whole blood and plasma sulfhydryl groups. Anal Biochem 93(1): 98-102 Furey WF, Robbins AH, Clancy LL, Winge DR, Wang BC, Stout CD (1986) Crystal structure of Cd, Zn metallothionein. Science 231: 704-710 Glaeser H, Coblenz A, Kruczek R, Ruttke I, Ebert-Jung A, Wolf K (1991) Glutathione metabolism and heavy metal detoxification in Schizosaccharomyces pombe: Isolation and characterization of glutathione-deficient, cadmium-sensitive mutants. Curr Genet 19: 207-213 Griffith OW, Meister A (1979) Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J Biol Chem 254: 7558-7560 Grill E, Gekeler W, Winnacker EL, Zenk MH (1986) Homo-phytochelatins are heavy metal-binding peptides of homo-GSH containing Fabales. FEBS Lett 197: 115-120 Grill E (1987) Phytochelatins, the heavy metal binding peptides of plants: characterization and sequence determination. Experientia Suppl 52: 317-322 Grill E, Loffler S, Winnacker EL, Zenk MH (1989) Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific g-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase). Proc Natl Acad Sci USA 86: 6838-6842 Grill E, Winnacker EL, Zenk MH (1985) Phytochelatins: the principal heavy-metal complexing peptides of higher plants. Science 230: 674-676 Grill E, Winnacker EL, Zenk MH (1991) Phytochelatins. Methods Enzymol 205: 333-341 Ha SB, Smith AP, Howden R, Dietrich WM, Bugg S, O'Connell MJ, Goldsbrough PB, Cobbett CS (1999) Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe. Plant Cell 11: 1153-1164 Hamer DH (1986) Metallothionein. Annu Rev Biochem 55: 913-951 Hayashi Y, Nakagawa CW, Murasugi A (1986) Unique properties of Cd-binding peptides induced in fission yeast, Schizosaccharomyces pombe. Environ Health Perspect 65: 13-19 (g-EC)nG in the cell- free system of the fission yeast. Biochem Cell Biol 69: 115-121 Hayashi Y, Morikawa S, Kawabata M, Hotta Y (1992) The synthesis of cadystins, heavy metal chelating peptides, is induced in the fission yeast by wounds of the cell wall or by incubation with chitosan. Biochem Biophy Res Commun. 188: 388-394 Hoffmann ED, Charette J, Stroobant V (1994) Mass Spectrometry, Principles and Applications, John Wiley & Sons, Inc., USA. Holleman AF, Wiberg E (1985) Lehrbuch der Anorganischen Chemie. Walter de Gruyter, Berlin, p. 868 Howden R, Andersen CR, Goldsbrough PB, Cobbett CS (1995a) A cadmium- sensitive, glutathione-deficient mutant of Arabidopsis thaliana. Plant Physiol 107: 1067-1073 Jackson PJ, Unkefer CJ, Doolen JA, Watt K, Robinson NJ (1987) Poly(gamma-glutamylcysteinyl)glycine: its role in cadmium resistance in plant cells. Proc Natl Acad Sci U S A 84: 6619-6623 Jazwinski SM (1990) Preparation of extracts from yeast. Methods Enzymol 182: 154-174 Klapheck S, Chrost S, Starke J, Zimmermann H (1992) g-Glutamylcysteinylserine: a new homologue of glutathione in plant of the family Poaceae. Bot Acta 105: 174-179 Klose J (1975) Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals. Humangenetik 26: 231-243 Kondo N, Isobe M, Imai K, Goto T (1983) Structure of cadystin, the unit-peptide of cadmium-binding pepttides induced in a fission yeast, Schizosaccharomyces pombe. Tetrahedron Lett 24: 925-928 Kramer U, Cotter-Howells JD, Charnock JM, Baker AJM, Smith JAC (1996) Free histidine as a metal chelator in plants that accumulate nickel. Nature 379: 635-638 Kubota H, Sato K, Yamada T, Maitani T (2000) Phytochelatin homologs induced in hairy roots of horseradish. Phytochemistry 53: 239-245 Li ZS, Lu YP, Zhen RG, Szczypka M, Thiele DJ, Rea PA (1997) A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalyzed transport of bis(glutathionato)cadmium. Proc Natl Acad Sci USA 94: 42-47 Liang ZY, Pilon-Smits EA, Jouanin L, Terry N (1999) Overexpression of glutathione synthetase in indian mustard enhances cadmium accumulation and tolerance. Plant Physiol 119: 73-80 Lovley DR, Coates JD (1997) Bioremediation of metal contamination. Curr Opin Biotechnol 8: 285-289 Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin Phenol Reagent. J Biol Chem 193: 265-275 Ma JF, Hiradate S, Matsumoto H (1997) Detoxifying aluminum with buckwheat. Nature 390: 569-570 Maret W (1994) Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange. Proc Natl Acad Sci USA 91: 237-241 Margoshes M, Vallee BL (1959) A cadmium protein from equine kidney cortex. J Am Chem Soc 79: 4813-4814 Meuwly P, Thibault P, Rauser WE (1993) g-Glutamylcysteinylglutamic acid - a new homologue of glutathione in maize seedlings exposed to cadmium. FEBS Lett 336: 472-476 Moffat AS, (1995) Plants proving their worth in toxic metal cleanup. Science 269: 302-303 Montgomery DM, Dean AC, Wiffen P, Macaskie LE (1995) Phosphatase production and activity in Citrobacter freundii and a naturally occurring, heavy-metal- accumulating Citrobacter sp. Microbiology 141: 2433-2441 Moore S, Stein WH (1963) Chromatographic determination of amino acid by the use of automatic recording equipment. Methods Enzymol 6: 819-931 Mutoh N, Hayashi Y (1988) Isolation of mutants of Schizosaccharomyces pombe unable to synthesize cadystin, small cadmium-binding peptides. Biochem Biophys Res Commun 151: 32-39 Nieboer E, Richardson DHS (1980) The replacement of the nondescript term heavy metals by a biological and chemically significant classification of metal ions. Environ Pollut Ser. B: 1-3 O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021 Ortiz DF, Kreppel L, Speiser DM, Scheel G, McDonald G, Ow DW (1992) Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter. EMBO J 11: 3491-3499 Ortiz DF, Ruscitti T, McCue KF, Ow DW (1995) Transport of metal-binding peptides by HMT1, a fission yeast ABC-type vacuolar membrane protein. J Biol Chem 270: 4721-4728 Pellet DM, Grunes DL, Kochian LV (1995) Organic acid exudation as an alumium-tolerance mechanism in maize (Zea mays L.) Planta 196: 103-110 Rabinowitz JC (1978) Analysis of acid-labile sulfide and sulfhydryl groups. Methods Enzymol 53: 273-275 Rauser WE (1990) Phytochelatin. Annu Rev Biochem 59: 61-86 Reese RN, Mehra RK, Tarbet EB, Winge DR (1988) Studies on the gamma-glutamyl Cu-binding peptide from Schizosaccharomyces pombe. J Biol Chem 263: 4186-4192 Rea PA, Vatamaniuk OK, Rigden DJ (2004) Weeds, worms, and more. Papain's long-lost cousin, phytochelatin synthase. Plant Physiol 136: 2463-2474 Rennenberg H (1989) Aspect of glutathione function and metabolism in plants. Plant Mol Biol 140: 279-292 Romanyuk ND, Rigden DJ, Vatamaniuk OK, Lang A, Cahoon RE, Jez JM, Rea PA (2006) Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase. Plant Physiol 141: 858-869 Ruotolo R, Peracchi A, Bolchi A, Infusini G, Amoresano A, Ottonello S (2004) Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis. J Biol Chem 279: 14686-14693 Ryan PR, Dehaize E, Randall PJ (1995b) Malate efflux from rootapices and tolerance to aluminum are highly correlated in wheat. Aust J Plant Physiol 22: 531-536 Salt DE, Wagner GJ (1993) Cadmium transport across tonoplast of vesicles from oat roots. J Biol Chem 268: 12297-12302 Salt DE, Smith RD, Raskin I (1998) Phytoremediation. Annu Rev Plant Physiol Plant Mol Biol 49: 643-668 Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379 Shih-Long Yan, Chien-Chieng Tsay, Yung-Reui Chen (2000) Isolation and characterization of phytochelatin synthase in rice seedlings. Proc. Natl. Sci. Counc. ROC 24:202-207 Speiser DM, Abrahamson SL, Banuelos G, Ow DW (1992) Brassica juncea produces a phytochelatin-cadmium-sulfide complex. Plant Physiol 99: 817-821 Strasdeit H, Duhme A.-K, Kneer R, Zenk MH, Hermes C, Nolting H.-F (1991) Evidence for discrete Cd(SCys)4 units in cadmium phytochelatin complexes from EXAFS spectroscopy. J Chem Soc Chem Commun 16: 1129-1130 Tsuji N, Nishikori S, Iwabe O, Matsumoto S, Shiraki K, Miyasaka H, Takagi M, Miyamoto K, Hirata K (2005) Comparative analysis of the two-step reaction catalyzed by prokaryotic and eukaryotic phytochelatin synthase by an ion-pair liquid chromatography assay. Planta 222: 181-191 Vatamaniuk OK, Mari S, Lu YP, Rea PA (1999) AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution. Proc Natl Acad Sci U S A 96: 7110-7115 Vatamaniuk OK, Mari S, Lu YP, Rea PA (2000) Mechanism of heavy metal ion activation of phytochelatin (PC) synthase. J Biol Chem 275: 31451-31459 Vatamaniuk OK, Bucher EA, Ward JT, Rea PA (2001) A new pathway for heavy metal detoxification in animals. Phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans. J Biol Chem 276: 20817-20820 Vivares D, Arnoux P, Pignol D (2005) A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis. Proc Natl Acad Sci U S A 102: 18848-18853 Vogeli-Lange R, Wagner GJ (1990) Subcellular localization of cadmium and cadmium-binding peptides in tobacco leaves. Plant Physiol 92: 1086-1093 Xiang C, Oliver DJ (1998) Glutathione metabolic genes coordinately respond to heavy metals and jasmonic acid in Arabidopsis. Plant Cell 10: 1539-1550 Zenk MH (1996) Heavy metal detoxification in higher plants - a review. Gene 179: 21-30 Zhu YL, Pilon-Smits EA, Tarun AS, Weber SU, Jouanin L, Terry N (1999) Cadmium tolerance and accumulation in Indian mustard is enhanced by overexpressing g-glutamylcysteine synthetase. Plant Physiol 121: 1169-1178 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/43508 | - |
| dc.description.abstract | 植物螯合素合成酶 (phytochelatin synthase, PCS) 利用 glutathione (GSH) 作為基質合成植物螯合素 (phytochelatin, PC)，以結合入侵植物的重金屬。過去研究指出，在六個不同物種中，PCS 序列在其 Tyr 55 相對胺基酸位置具有半保守性，該位置胺基酸非 Tyr 即 Phe，都含有芳香族基團。實驗發現 AtPCS1 (Y55A) 突變株的活性也下降，代表 Tyr 55 在 PCS 活性中扮演重要角色。在 Tyr 55 可能利用鎘離子作為架橋，將第二個 PCS 帶至基質結合區，以進行催化作用的假說下，我們建構了七種 Tyr 55 突變株。包括五株全長 PCS：AtPCS1 (Y55A), AtPCS1 (Y55D), AtPCS1 (Y55E), AtPCS1 (Y55H) 及 AtPCS1 (Y55F)；與兩株 PCS 的 N-端部份：AtPCS1-N (Y55E) 及 AtPCS1-N (Y55W)。表現之後再進行各種 PCS 蛋白質的活性測定。AtPCS1 (Y55D) 突變株和 AtPCS1 (Y55E) 突變株的活性都下降了，然而若以鎘離子對 GSH 做預處理，它們的活性增加程度比 AtPCS1 (Y55A) 增加程度高出許多。更甚者，以經過 Cd 預處理的 GSH 作為基質，AtPCS1 (Y55H) 的活性不增反減，代表了帶電性質能夠調控 PCS 活性。有趣的是，突變株 AtPCS1-N (Y55W) 沒有出現 PCS 活性，但若將基質 GSH 以 Cd 做預處理，便能回復些微活性，說明了 Trp 可能給活性區帶來立體空間障礙，但是在芳香環陽離子-pi 電子交互作用的幫助下，能回復部分活性。總之，Tyr 55 的芳香帶電性質以及立體空間結構，對 PCS 活性具有重要影響。 | zh_TW |
| dc.description.abstract | Using glutathione (GSH) as the substrate, phytochelatin synthase (PCS, EC 2.3.2.15) catalyzes the synthesis of phytochelatins (PCs) which could bind heavy metals in the plant cell. It was found that the corresponding amino acids of Tyr 55 on the PCS sequences are semi-conserved among six different species. The positions are occupied either by Tyr or Phe with aromatic side chains. In vitro experiments showed that PCS activity decreased in the mutant of AtPCS1 (Y55A) revealing that Tyr 55 is essential for PCS activity. Under the hypothesis that Tyr 55 might play a role in docking the gamma-EC of the second GSH substrate by using Cd as the bridge, site-directed mutagenesis on Tyr 55 has been performed. We constructed five mutants for the full-length AtPCS1: AtPCS1 (Y55A), AtPCS1 (Y55D), AtPCS1 (Y55E), AtPCS1 (Y55H) and AtPCS1 (Y55F); and two mutants for the N-terminal part of PCS (AtPCS1-N): AtPCS1-N (Y55E) and AtPCS1-N (Y55W). After expression of the proteins, the enzymes were analyzed for PCS activity. The activity of the mutants AtPCS1 (Y55D) and AtPCS1 (Y55E) decreased; however, by the addition of Cd with substrate GSH in the pretreatment, AtPCS1 (Y55A) showed higher increase in its activity. Furthermore, the activity of AtPCS1 (Y55H) decreased when pretreated with Cd. These observations indicated that the charge of the substrate might play a role in regulating PCS activity. Interestingly, the mutant AtPCS1-N (Y55W) had no PCS activity; however, by the addition of GSH pretreated with Cd, its activity increased slightly, showing that Trp might provide stereo hindrance near the active site, but the activity could be restored by the support of strong cation-p interaction with Cd by its aromatic ring. In conclusion, the aromatic ring on Tyr 55 might be critical for PCS activity. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T02:22:36Z (GMT). No. of bitstreams: 1 ntu-98-R95b47216-1.pdf: 2404605 bytes, checksum: 5d81fa400dfcc66cb98510edc98adfe8 (MD5) Previous issue date: 2009 | en |
| dc.description.tableofcontents | 第一章 緒論 7
1.1 重金屬污染 7 1.1.1 重金屬的定義 7 1.1.2 重金屬對生物體造成之傷害 8 1.1.3 鎘對人體造成的傷害 8 1.1.4 以生物復育法清除重金屬污染 9 1.2 生物抗重金屬機制 11 1.2.1 金屬硫蛋白 11 1.2.2 植物螯合素 13 1.2.3 細胞對重金屬的其他解毒機制 14 1.3 植物螯合素生合成 15 1.3.1 植物螯合素與鎘結合形成複合體 17 1.3.2 鎘複合物是由液泡膜上的 HMT1 蛋白質運送至液泡內 18 1.4 植物螯合素合成酶 19 1.4.1 植物螯合素合成酶之基因序列 20 1.4.2 植物螯合素合成酶之作用機制 21 1.4.3 植物螯合素合成酶是一種 dipeptidyltransferase 25 1.4.4 植物螯合素合成酶屬於 papain superfamily protease 27 1.5 基因重組宿主/載體系統的種類及選擇 30 1.5.1 宿主的分類 30 1.5.2 影響重組蛋白表現之因子 31 1.5.3 原核系統表現 34 1.5.4 真核系統表現 34 1.6 實驗緣起及研究目標 35 第二章材料與方法 36 2.1 材料 36 2.1.1 菌株 36 2.1.2 載體 36 2.2 表現載體之建構 37 2.2.1 核酸引子之設計： 37 2.2.2 聚合酶鏈鎖反應 (polymerase chain reaction, PCR) 38 2.2.3 PCR 產物純化 (PCR Clean-UP) 39 2.2.4 限制酶酶切反應 40 2.2.5 質體之轉形 (Transformation) 42 2.2.6 質體 DNA 之小量分離 42 2.3 重組蛋白質之誘導與表現 43 2.3.1 最佳誘導時間、溫度與 IPTG 誘導濃度 43 2.3.2 重組蛋白質之表現 45 2.3.3 重組蛋白質之純化 45 2.4 電泳檢定法 47 2.4.1 SDS膠體電泳 47 2.4.2 膠體染色法 51 2.4.3 膠片乾燥法及護貝 52 2.4.4 蛋白質電泳轉印法 54 2.5 一般分析法 56 2.5.1 蛋白質定量法 56 2.6 PCS 活性分析 47 2.6.1 SDS膠體電泳 57 2.7 酵素免疫染色法 59 第三章 結果與討論 62 3.1 不同片段植物螯合素合成酶 PCS 表現載體之建構 62 3.1.1 AtPCS1 及 AtPCS1-N 突變株之建立 62 3.1.2 最適表現條件之探討 63 3.1.3 重組蛋白之表現及純化 64 3.2 重組蛋白質 AtPCS1 及 AtPCS1-N 野生株之活性分析 68 3.2.1 AtPCS1 及 AtPCS1-N 之野生株活性分析 68 3.2.2 AtPCS1 及 AtPCS1-N 野生株活性與不同金屬離子之關係 69 3.3 重組表現蛋白質 AtPCS1 及 AtPCS1-N 突變株之活性分析 70 3.3.1 AtPCS1 Tyr 55 突變株之活性分析 71 3.3.2 AtPCS1-N Tyr 55 突變株之活性分析 73 第四章結論 75 4.1 已建立的保存載體 75 4.2 Tyr 55 位置對 PCS 活性很重要 75 4.3 未來展望 76 參考文獻 77 | |
| dc.language.iso | zh-TW | |
| dc.subject | Tyr 55 | zh_TW |
| dc.subject | 植物螯合素合成酶 | zh_TW |
| dc.subject | 阿拉伯芥 | zh_TW |
| dc.subject | 突變株 | zh_TW |
| dc.subject | Mutants | en |
| dc.subject | Arabidopsis thaliana | en |
| dc.subject | Phytochelatin Synthase | en |
| dc.subject | Tyr 55 | en |
| dc.title | 阿拉伯芥植物螯合素合成酶 Tyr 55 突變株重組蛋白之表現與活性分析 | zh_TW |
| dc.title | Expression and Activity Analysis of Tyr 55 Mutants of Phytochelatin Synthase from Arabidopsis thaliana | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 97-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 楊健志(Chien-Chih Yang),張世宗(Shih-Chung Chang),吳建興(Jian-Shing Wu),陳翰民(Han-Min Chen) | |
| dc.subject.keyword | 阿拉伯芥,植物螯合素合成酶,Tyr 55,突變株, | zh_TW |
| dc.subject.keyword | Arabidopsis thaliana,Phytochelatin Synthase,Tyr 55,Mutants, | en |
| dc.relation.page | 86 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2009-08-19 | |
| 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 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-98-1.pdf 未授權公開取用 | 2.35 MB | Adobe PDF |
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。