請用此 Handle URI 來引用此文件：
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/47283完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 周宏農 | |
| dc.contributor.author | Shu-Yin Lin | en |
| dc.contributor.author | 林書吟 | zh_TW |
| dc.date.accessioned | 2021-06-15T05:53:30Z | - |
| dc.date.available | 2010-08-20 | |
| dc.date.copyright | 2010-08-20 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-08-18 | |
| dc.identifier.citation | 洪雅萍，1994。溫度、光線對杉葉紫菜絲狀體光合色素組成的影響，國立中興大學植物研究所碩士論文。
鄭俊明，1992。紅藻絲狀體藻膽蛋白之高效層析及光譜之研究，國立台灣大學漁業科學研究所碩士論文。 鄭俊明，1999。頭髮菜藻紅蛋白異價體分析研究，國立台灣大學海洋研究所博士論文。 Airth R.L. and Blinks L.R., 1956. A new phycoerythrin from Porphyra naiadum. Biol. Bull. 3, 321–327. Baker N.R., 1991. A possible role for photosystem II in environmental perturbations of photosynthesis. Physiol. Plant. 81, 563–570. Bhat V.B., Gaikwad W.N. and Madyastha K.M., 1998. Hepatoprotective effect of C- phycocyanin for carbon tetrachloride and R-(+)-pulegone-mediated hepatotoxicity in rats. Biochem. Bioph. Res. Co. 249, 428–431. Bhat V.B. and Madyastha K.M., 2000. C-phycocyanin: a potent peroxyl radial scaven-ger in vivo and in vitro. Biochem. Biophys. Res. Comm. 275, 20–25. Boussiba S. and Richmond A.E., 1980. C-phycocyanin as a storage protein in the blue- green alga Spirulina platensis. Arch. Microbiol. 125, 143–147. Broom J.E.S., Farr T.J. and Nelson W.A., 2004. Phylogeny of the Bangia flora of New Zealand suggests a southern origin for Porphyra and Bangia (Bangiales, Rhodo-phyta). Mol. Phylogenet. Evol. 31, 1197–1207. Brown A.S. and Troxler R.F., 1977. Properties and N-terminal sequence of allophyco-cyanin from the unicellular Rhodophyte Cyanidium caldarium. Biochem. J. 163, 571–581. Chapman D.J., Cole W.J. and Siegelman H.W., 1967. Chromophores of allophycocyanin and R-phycocyanin. Biochem. J. 105, 903–905. Chen L.C.M., Edelstein T. and McLachlan J., 1969. Bonnemaisonia hamifera Hariot in nature and in culture. J. Phycol. 5, 211–220. Cherng S.C., Cheng S.N., Tarn A. and Chou T.C., 2007. Anti-inflammatory activity of c-phycocyanin in lipopolysaccharide-stimulated RAW 264.7 macrophages. Life Sci. 81, 1431–1435. Chiang Y.M., 1962. Marine algae of northern Taiwan (Rhodophyta). Taiwania 8, 143–165. Chiang Y.M., 1972. Keys to the genera of marine algae of Taiwan. Taiwania 17, 8–13. Chiang Y.M. and Chou H.N., 2004. Method of Porphyra dentata for producing high OD phycoerythrin. TW. Patent 223000B, 21 November 2004. Chou H.N. and Jeng J.M., 1993. High performance liquid chromatography of biliprotein from Bangia atropurpurea ‘Conchocelis’. Hydrobiologia 260/261, 571–576. D'Agnolo E., Rizzo R., Paoletti S. and Murano E., 1994. R-phycoerythrin from the red alga Gracilaria longa. Phytochemistry 35, 693–696. Duan D.L., Fei X.G., Ren H.X., Chen X. and Zhu Y., 1995. Effect of cytokinins and auxins on the growth of free-living conchocelis of Porphyra yezoensis. Chin. J. Oceanol. Limnol. 13, 266–270. Eriksen N.T., 2008. Production of phycocyanin—a pigment with applications in biology, biotechnology, foods and medicine. Appl. Microbiol. Biotechnol .80, 1–14. Esenbeck N., 1836. Ueber einen blau-rothen Farbstoff, der sich bei der Zersetzung von Oscillatorien bildet. Liebigs. Ann. Chem. 17, 75–82. (cited from Tandeau de Marsac, 2005) Everroad C., Six C., Partensky F., Thomas J.C., Holtzendorff J. and Wood A.M., 2006. Biochemical bases of type IV chromatic adaptation in marine Synechococcus spp. J. Bacteriol. 188, 3345–3356. Fujiwara-Arasaki T., Yamamoto M. and Kakiuchi K., 1985. C-phycocyanin from a red alga, Porphyra tenera: subunit structure. Biochim. Biophys. Acta. 828, 261–265. Gantt E., 1981. Phycobilisomes. Ann. Rev. Plant Physiol. 32, 327–347. Gantt E. and Conti S.F., 1965. The ultrastructure of Porphyridium cruentum. J. Cell Bi-ol. 26, 365–381. Gantt E. and Conti S.F., 1966. Granules associated with the chloroplast lamellae of Porphyridium cruentum. J. Cell Biol. 29, 423–434. Gantt E. and Conti S. F., 1969. Ultrastructure of blue-green algae. J. Bacteriol. 97, 1486–1493. Gantt E. and Lipschultz C.A., 1974. Phycobilisomes of Porphyridium cruentum: pig-ment analysis. Biochem. 13, 2960–2966. Glazer A.N., 1981. Photosynthetic accessory proteins with bilin prosthetic groups. In: Hatch M.D. and Boardman N.K. (Eds) The Biochemistry of Plants. Vol. 8, Photo-synthesis. Academic Press, New York, pp. 51–96. Glazer A.N., 1985. Light harvesting by phycobilisomes. Ann. Rev. Biophys. Chem. 14, 47–77. Glazer A.N., 1989. Light Guides. J. Biol. Chem. 264, 1–4. Glazer A.N., 1994. Phycobiliproteins - a family of valuable, widely used fluorophores. J. Appl. Phycol. 6, 105–112. Glazer A.N. and Hixson C.S., 1975. Characterization of R-phycocyanin. Chromophore content of R-phycocyanin and C-phycoerythrin. J. Biol. Chem. 250, 5487–5495. Glazer A.N. and Hixson C.S., 1977. Subunit structure and chromophore composition of rhodophytan phycoerythrins. Porphyridium cruentum B-phycoerythrin and b-phycoerythrin. J. Biol. Chem. 252, 32–42. Haxo F., O’hEocha C. and Norris P., 1955. Comparative studies of chromatographically separated phycoerythrins and phycocyanins. Arch. Biochem. Biophys. 1955, 162–173. Huang B., Wang G.C., Zeng C.K. and Li Z.G., 2002. The experimental research of R- phycoerythrin subunits on cancer treatment - a new photosensitizer in PDT. Cancer Biother. Radio. 17, 35–42. Inskeep W.P. and Bloom P.R., 1985. Extinction coefficients of chlorophyll a and b in N,N-Dimethylformamide and 80% acetone. Plant Physiol. 77, 483–485. Isailovic D., Li H.W. and Yeung E.S., 2004. Isolation and characterization of R-phycoerythrin subunits and enzymatic digests. J. Chromatogr. A 1051, 119–130. Izydorczyk K., Tarczynska M., Jurczak T., Mrowczynski J. and Zalewski M., 2005. Measurement of phycocyanin fluorescence as an online early warning system for cyanobacteria in reservoir intake water. Environ. Tox. 20, 425–430. Jiang T., Zhang J.P., Chang W.R., and Liang D.C., 2001. Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome. Biophys. J . 81, 1171–1179. Karsten U. and West J.A., 2000. Living in the intertidal zone — seasonal effects on he-terosides and sun-screen compounds in the red alga Bangia atropurpurea (Bangiales). J. Exp. Mar. Biol. Ecol. 254, 221–234. Kehoe D. M. and Gutu A., 2006. Responding to color: the regulation of complementary chromatic adaptation. Annu. Rev. Plant Biol. 57, 127–150. Kim N.G., 1999. Culture studies of Porphyra dentata and P. pseudolinearis (Bangiales, Rhodophyta), two dioecious species from Korea. Hydrobiologia 398/399, 127–135. Kursar T.A. and Alberte R.S., 1983. Photosynthetic unit organization in a red alga. Re-lationships between light-harvesting pigments and reaction centers. Plant Physiol. 72, 409–414. Lemberg R., 1928. Die chromoproteide der rotalgen. I. Liebigs. Ann.Chem. 461, 46–89. (cited from Tandeau de Marsac, 2005) Lemberg R., 1930. Chromoproteide der Rotalgen. II. Spaltung mit pepsin un sauren. Isolierung eines pyrrolfarbstoffs. Liebigs. Ann. Chem. 477, 195–245. (cited from Tandeau de Marsac, 2005) Lewis J.E. and Norris J.N., 1987. A history annotated account of the benthic marine al-gae of Taiwan. Smithsonian institution Press, Washington, D.C. 48 pp. Lewitus A.J. and Caron D.A., 1990. Relative effects of nitrogen or phosphorus deple-tion and light intensity on the pigmentation, chemical composition, and volume of Pyrenomonas salina (Cryptophyceae). Mar. Ecol. Prog. Ser. 61, 171–181. Lin R.L. and Stekoll M.S., 2007. Effects of plant growth substances on the conchocelis phase of Alaskan Porphyra (Bangiales, Rhodophyta) species in conjunction with en-vironmental variables. J. Phycol. 43, 1094–1103. Lindstrom S.C., Conitz J.M., Hall S. and Stekoll M.S., 2008. Induction of conchospore release: ecotypic variation in northeast Pacific species of Porphyra. J. Appl. Phycol. 20, 331–340. Liu J.Y., Jiang T., Zhang J.P. and Liang D.C., 1999. Crystal structure of allophycocya-nin from red algae Porphyra yezoensis at 2.2-Å resolution. J Biol. Chem. 274, 16945–16952. Long S.P. and Humphries S., 1994. Photoinhibition of photosynthesis in nature. Annu. Rev. Plant Physial. Plant Mol. Biol. 45, 633–662. Lowry O.H., Rosebrough N.J., Farr A.L. and Randall R.J., 1951. Protein measurement with the Folin phenol reagent. J. biol. chem. 193, 265–275. Ma Y.H., Xie J., Zhang R., Hu C.C. and Zhao J.Q., 2008. Molecular properties of R-phycocyanin subunits from Polysiphonia urceolata in potassium phosphate buffer. Photochem. Photobiol. Sci. 7, 263–268. MacColl R. and Guard-Friar D., 1987. Phycobiliproteins. CRC Press, Florida. 218 pp. MacColl R., Eisele L.E., Williams E.C. and Bowser S.S., 1996. The discovery of a novel R-phycoerythrin from an antarctic red alga. J. Biol. Chem. 271, 17157–17160. McCarty M.F., 2007a. “Iatrogenic Gilbert syndrome”—a strategy for reducing vascular and cancer risk by increasing plasma unconjugated bilirubin. Med. Hypotheses 69, 974–994. McCarty M.F., 2007b. Clinical potential of Spirulina as a source of phycocyanobilin. J. Med. Food 10, 566–570. Mihova S.G., Georgieva D.I., Minkova K.M. and Tchernovb A.A., 1996. Phycobili-proteins in Rhodella reticulata and photoregulatory effects on their content. J. Bio-technol. 48, 251–257. Mirkovic T., Wilk K.E., Curmi P.M.G. and Scholes G.D., 2009. Phycobiliprotein diffu-sion in chloroplasts of cryptophytes Rhodomonas CS24. Photosynth. Res. 100, 7–17. Morel A., 1978. Available, usable, and stored radiant energy in relation to marine pho-tosynthesis. Deep Sea Res. 25, 673–688. Nagaoka S., Shimizu K., Kaneko H., Shibayama F., Morikawa K., Kanamaru Y., Otsu-ka A., Hirahashi T. and Kato T., 2005. A novel protein C-phycocyanin plays a crucial role in the hypocholesterolemic action of Spirulina platensis concentrate in rats. J. Nutr. 135, 2425–2430. Notoya M. and Kikuchi N., 1993. Bangia atropurpurea. In: Hori T. (Ed.) An illustrated atlas of the life history of algae. Vol. 2, Brown and Red Algae, Uchida Rokakuho Publishing, Tokyo, pp. 198–199. Notoya M. and Iijima N., 2003. Life history and sexuality of archeospore and apogamy of Bangia atropurpurea (Roth) Lyngbye (Bangiales, Rhodophyta) from Fukaura and Enoshima, Japan. Fisheries Sci. 69, 799–805. O’hEocha C., 1958. Comparative biochemical studies of the phycobilins. Arch. Biochem. Biophys. 73, 207–219. O’hEocha C., 1965. Biliproteins of algae. Ann. Rev. Plant Physiol. 16, 415–434. Ong L.J. and Glazer A.N., 1987. R-phycocyanin II, a new phycocyanin occurring in marine Synechococcus species. Identification of the terminal energy acceptor bilin in phycocyanins. J. Biol. Chem. 262, 6323–6327. Oi V.T., Glazer A.N. and Stryer L., 1982. Fluorescent phycobiliprotein conjugates for analyses of cells and molecules. J. Cell. Biol. 93, 981–986. Orfanidis S., 2001. Culture Studies of Porphyra leucosticta (Bangiales, Rhodophyta) from the Gulf of Thessaloniki, Greece. Bot. Mar. 44, 533–539. Rennis D.S. and Ford T.W., 1992. A survey of antigenic difference between phycoeryt-hrins of various red alga (Rhodophyta) species. Phycologia. 32,192–204. Roy K.R., Arunasree K.M., Reddy N.P., Dheeraj B., Reddy G.V. and Reddanna P., 2007. Alteration of mitochondrial membrane potential by Spirulina platensis C-phycocyanin induces apoptosis in the doxorubicin-resistant human hepatocellu-lar-carcinoma cell line HepG2. Biotechnol. Appl. Biochem. 47,159–167. Scarabel L., Camuccio P., Foltran A., Maranzana G., Talarico L., Rascio N. and An-dreoli C., 1996. Thalli of Plocamium cartilagineum (L.) Dixon (Gigartinales, Rho-dophyta) growing at two different depths. Giorn. Bot. Ital. 130, 690–693. Scheer H., 1981. Biliproteins. Angew. Chem. Int. Ed Engl. 20, 241–261. Scheer H. and Zhao K.H., 2008. Biliprotein maturation: the chromophore attachment. Mol. Microbiol. 68, 263–276. Schneider S., Jiiger W., Prenzel C.J., Brehm G., Maruthi Sai P.S., Scheer H. and Lottspeich F., 1994. Photophysics of phycoerythrocyanins from the cyanobacterium Westiellopsis prolifica studied by time-resolved fluorescence and coherent anti-Stokes Raman scattering spectroscopy. J. Photoch. Photobio. B. 26, 75–85. Seib L.O. and Kehoe D.M., 2002. A turquoise mutant genetically separates expression of genes encoding phycoerythrin and its associated linker peptides. J. Bacteriol. 184, 962–970. Sekar S. and Chandramohan M., 2008. Phycobiliproteins as a commodity: trends in ap-plied research, patents and commercialization. J. Appl. Phycol. 20, 113–136. Shih S.R., Tsai K.N., Li Y.S., Chueh C.C. and Chan E.C., 2003. Inhibition of enterovi-rus 71-induced apoptosis by allophycocyanin isolated from a blue-green alga Spiru-lina platensis. J. Med. Virol. 70, 119–125. Sidler W., 1994. Phycobilisome and phycobiliprotein structures. In: Bryant D.A. (Ed.) The Molecular Biology of Cyanobacteria, Kluwer Academ. Publ., Dordrecht, pp. 140–205. Simis S.G.H., Peters S.W.M. and Gons H.J., 2005. Remote sensing of the cyanobacteri-al pigment phycocyanin in turbid inland water. Limnol. Oceanogr. 50, 237–245. Sode K.J., Horikoshi K., Takeyama J., Nakamura N. and Matsunga T., 1991. On line monitoring of marine cyanobacterial cultivation based on phycocyanin fluorescence. J. Biotechnol. 21, 209–218. Sommerfeld M.R. and Nichols H.W., 1970. Developmental and cytological studies of Bangia fuscopurpurea in culture. Am. J. Bot. 57, 640–648. Sorby H.C., 1877. On the characteristic colouring-matters of the red groups of algae. J. Linnean. Soc. Bot. 15, 34–40. (cited from Tandeau de Marsac N., 2005) Stekoll M.S., Lin R.L. and Lindstrom S.C., 1999. Porphyra cultivation in Alaska: con-chocelis growth of three indigenous species. Hydrobiologia 398/399, 291–297. Stoscheck C.M., 1990. Quantitation of Protein. Methods Enzymol. 182, 50–68. Subhashini J., Mahipal V.K., Reddy M.C., Reddy M.M., Rachamallu A. and Reddanna P., 2004. Molecular mechanisms in C-phycocyanin induced apoptosis in human chronic myeloid leukemia cell line-K562. Biochem. Pharmacol. 68, 453–462. Sun L., Wang S.M., Chen L.X. and Gong X.Q., 2003. Promising fluorescent probes from phycobiliproteins. IEEE J. Sel. Top. Quant. 9, 177–188. Svedberg T. and Katsurai T., 1929. The molecular weights of phycocyan and of phy-coerythrin from Porphyra tenera and of phycocyan from Aphanizomenon flos-aquae. J. Am. Chem. Soc. 51, 3573–3583. Talarico L., 1996. Phycobiliproteins and phycobilisomes in red algae: adaptative res-ponses to light. Sci. Mar. 60 suppl., 205–222. Talarico L. and Maranzana G., 2000. Light and adaptive responses in red macroalgae: an overview. J. Photoch. Photobio. B. 56, 1–11. Tandeau de Marsac N., 1977. Occurrence and nature of chromatic adaptation in cyano-bacteria. J. Bacteriol. 130, 82–91. Tandeau de Marsac N., 2005. Phycobiliproteins and phycobilisomes: the early observa-tions. In: Govindjee, Beatty J.T., Gest H. and Allen J.F. (Eds.) Discoveries in Photo-synthesis, Springer Netherlands, Netherlands, pp. 443–451. Tandeau de Marsac N. and Cohen-Bazire G., 1977. Molecular composition of cyano-bacterial phycobilisomes. Proc. Natl. Acad. Sci. USA 74, 1635–1639. Teale F.W.J. and Dale R.E., 1970. Isolation and spectral characterization of phycobili-proteins. Biochem. J. 116, 161–169. Telford W.G., Moss M.W., Morseman J.P. and Allnutt F.C.T., 2003. Cyanobacterial stabilized phycobilisomes as fluorochromes for extracellular antigen detection by flow cytometry. J. Immunol. Methods 254, 13–30. van Tussenbroek B.I., 1984. Effect of continuous unilateral irradiation on the conchoce-lis of Porphyra umbilicalis (L.) J. Ag. and some other red algae. J. Exp. Mar. Biol. Ecol. 83, 263–274. Wang W.J., Zhu J.Y., Xu P., Xu J.R., Lin X.Z., Huang C.K., Song W.L., Peng G., and Wang G.C., 2008. Characterization of the life history of Bangia fuscopurpurea (Bangiaceae, Rhodophyta) in connection with its cultivation in China. Aquaculture 278, 101–109. Wedemayer G.J., Wemmer D.E. and Glazer A.N., 1991. Phycobilins of cryptophycean algae. Structures of novel bilins with acryloyl substituents from phycoerythrin 566. J. Biol. Chem. 266, 4731–4741. Wedemayer G.J., Kidd D.G., Wemmer D.E. and Glazer A.N., 1992. Phycobilins of cryptophycean algae. Occurrence of dihydrobiliverdin and mesobiliverdin in cryp-tomonad biliproteins. J. Biol. Chem. 267, 7315–7331. Woolcott G.W. and King R.J., 1998. Porphyra and Bangia (Bangiaceae, Rhodophyta) in warm temperate waters of eastern Australia: Morphological and molecular analyses. Phycoi. Res. 46, 111–123. Zeng F.J., Yang Z.X. and Jiang L.J., 1984. Isolation and characterization of R-phycocyanin from Polysiphonia urceolata. Hydrobiologia 116/117, 594–596. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/47283 | - |
| dc.description.abstract | R型藻藍蛋白 (R-phycocyanin, R-PC) 與R型藻紅蛋白 (R-Phycoerythrin, R-PE)、異藻藍蛋白 (Allophycocyanin, APC) 同為紅藻中光合作用的輔助色素，可作為螢光標誌應用於醫事檢驗試劑或天然染料應用於食品、化妝品色素。由於最近發現到其在醫療上的活性，擬對此蛋白質特徵進一步研究。藉由頭髮菜B. atropurpurea絲狀體的培養，冷凍乾燥藻體磨粉後以磷酸緩衝液萃取，經梯度飽和硫酸銨沉澱後，再經膠濾製備層析排除大量R-PE後，以羥基磷酸石灰管柱層析配合逐漸提高磷酸緩衝液濃度的方式沖提，純化出R-PC，其在618 nm與280 nm波長吸收的比值 (A618/A280) 為4.11，R-PC吸收光譜有兩個吸收高峰，分別位於553 nm及618 nm，使用618 nm波長激發，可在640 nm處獲得最大螢光強度。R-PC的SDS-PAGE呈現兩明顯之色帶：17.40 kDa與21.72 kDa，顯示其與文獻相符之α和β次單元體，這些證據顯示所設計的分離操作可以獲得高純度的PC，其回收率約為22.0%。在純化R型藻藍蛋白的過程中，同時成功純化了A565/A280為6.14之R型藻紅蛋白與A650/A280為4.18之異藻藍蛋白，R型藻紅蛋白有明顯的三個吸收峰，位於497 nm、543 nm及565 nm，並釋出波長在574 nm之螢光，異藻藍蛋白的最大吸收值位於650 nm，於618 nm附近有一肩峰，於664 nm處得到最大釋放螢光強度，皆與文獻相符。利用純質藻膽蛋白溶液於565 nm、618 nm及650 nm之吸收，求其於此三波長處之消光係數，建立從藻膽蛋白粗萃混合液中估算各藻膽蛋白含量之運算公式，並將其試用於比較不同光質對於色素含量之影響。從不同光質 (白光、藍光、綠光和紅光) 對頭髮菜絲狀體生長與色素含量的實驗結果中發現，以白光、藍光及綠光培養之頭髮菜絲狀體生長情形較以紅光培養者為佳，在培養22天後，不同光質對於頭髮菜絲狀體R型藻紅蛋白含量之影響沒有顯著差異，藍光及紅光會促進其R型藻藍蛋白與異藻藍蛋白的合成，綠光則是增加其葉綠素a的含量。 | zh_TW |
| dc.description.abstract | R-phycocyanin, R-PC, R-phycoerythrin, R-PE and allophycocyanin, APC are the photosynthetic accessory pigments of the red algae. As good fluorescent pigments and natural dyes, they have been applied in food, cosmetics and medical diagnostic reagents. Recently we found the immunological modulation bioactivity of R-PC, so as, tried to isolate more of this protein for further characterization studies. In this study, the Con-chocelis phase of Bangia atropurpurea was used for phycobiliprotein extraction. Am-monium sulfate salting-out and gel filtration chromatography, alter a series of R-PC was isolated and subject to a chromatographic purification by a hydroxylapatite column with a two-step gradient elution of K-phosphate buffers. Pure R-PC obtained had an absorb-ance ratio A618/A280 of 4.11. The purple fluorescent protein, R-PC was identified by its two major absorption peaks at 553 and 618 nm. The emission spectra of R-PC obtained had a maximal peak at 640 nm under excitation at 618 nm. From SDS-PAGE, R-PC was determined to consist of α and β subunits of molecular weights of 17.40 and 21.72 kDa, respectively. Both gel electrophoresis and spectroscopic data showed the purity of R-PC through the designed operation. In the same process, fractions, obtained alter gel filtration (A565/A280=6.14), showed the typical spectroscopic characters of R-PE, maxi-mal absorptions were detected at 497, 543 and 565 nm and emission at 574 nm. Allo-phycocyanin was also obtained with fractions (A650/A280=4.18) after R-PC in separation and determined the maximal absorption at 650 nm and emission 660 nm. In order to know the effect of light quality on the growth and comparison of biliproteins, B. atro-purpurea Conchocelis cultures were exposed to white, blue, green and red light in a 22-days experiment. Red light resulted in the lowest production of algal biomass and blue and green light illumination had no different in growth from the white light. R-phycoerythrin content was not affected by light quality, whereas R-phycocyanin and allophycocyanin content were enhanced by blue or red light. Green light increased the content of chlorophyll a. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T05:53:30Z (GMT). No. of bitstreams: 1 ntu-99-R95b45004-1.pdf: 5310065 bytes, checksum: f59195a174a5fdec5c47e9796aef6a60 (MD5) Previous issue date: 2010 | en |
| dc.description.tableofcontents | 致謝...................................................... i
中文摘要................................................. ii 英文摘要................................................ iii 目錄...................................................... v 表目錄.................................................. vii 圖目錄................................................. viii 第一章 前言............................................ 1 第二章 文獻回顧 2.1 藻膽蛋白與藻膽體..................................... 6 2.2 藻藍蛋白的分類....................................... 9 2.3 藻膽蛋白的應用與醫藥潛力............................ 10 2.4 光質調適 (Chromatic adaptation)..................... 13 第三章 材料與方法 3.1 頭髮菜絲狀體之來源與培養............................ 15 3.2 藻膽蛋白之提純 3.2.1 藻膽蛋白之萃取................................... 15 3.2.2 藻紅蛋白之純化(膠濾層析)......................... 16 3.2.3 藻藍蛋白與異藻藍蛋白之純化(羥基磷酸石灰管柱層析). 16 3.3 藻膽蛋白光譜學性質及定量 3.3.1 藻膽蛋白光譜性質................................. 17 3.3.2 蛋白質濃度的測定................................. 17 3.3.3 藻膽蛋白消光係數之測量計算....................... 18 3.3.4 藻膽蛋白混合液之藻膽蛋白含量估計................. 18 3.4 膠體電泳分析 3.4.1 原態聚丙烯醯胺膠體電泳分析....................... 19 3.4.2 SDS-聚丙烯醯胺膠體電泳分析....................... 19 3.5 不同光質對頭髮菜絲狀體生長及色素含量的影響 3.5.1 不同光質之處理................................... 20 3.5.2 生長測定......................................... 20 3.5.3 藻膽蛋白含量的測定............................... 20 3.5.4 葉綠素a含量的測定................................ 21 3.5.5 資料分析......................................... 21 第四章 結果與討論 4.1 頭髮菜B. atropurpurea絲狀體藻膽蛋白之提純 4.1.1 藻膽蛋白之萃取................................... 22 4.1.2 藻紅蛋白之純化與分析............................. 22 4.1.3 藻藍蛋白之純化與分析............................. 23 4.1.4 異藻藍蛋白之純化與分析........................... 24 4.2 頭髮菜絲狀體藻膽蛋白光譜學定量 4.2.1 藻膽蛋白消光係數之測量........................... 25 4.2.2 藻膽蛋白混合液之藻膽蛋白含量估計運算公式......... 26 4.3 不同光質對頭髮菜絲狀體生長及色素含量的影響 4.3.1 不同光質對頭髮菜絲狀體生長的影響................. 27 4.3.2 不同光質對頭髮菜絲狀體色素含量的影響............. 28 參考文獻................................................. 34 表....................................................... 47 圖....................................................... 57 | |
| dc.language.iso | zh-TW | |
| dc.subject | 光質 | zh_TW |
| dc.subject | R型藻藍蛋白 | zh_TW |
| dc.subject | 絲狀體 | zh_TW |
| dc.subject | 藻膽蛋白 | zh_TW |
| dc.subject | 純化 | zh_TW |
| dc.subject | 頭髮菜 | zh_TW |
| dc.subject | light quality | en |
| dc.subject | R-phycocyanin | en |
| dc.subject | Bangia atropurpurea | en |
| dc.subject | Conchocelis phase | en |
| dc.subject | phycobiliprotein | en |
| dc.subject | purification | en |
| dc.title | 頭髮菜絲狀體R型藻藍蛋白之提純與性質分析及光質對其生長與色素含量的影響 | zh_TW |
| dc.title | Purification and Characterization of R-phycocyanin from Bangia atropurpurea Conchocelis and the Effects of Different Light Qualities on the Growth and Pigment Contents | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 江永棉,鄭俊明,李宗徽 | |
| dc.subject.keyword | R型藻藍蛋白,頭髮菜,絲狀體,藻膽蛋白,純化,光質, | zh_TW |
| dc.subject.keyword | R-phycocyanin,Bangia atropurpurea,Conchocelis phase,phycobiliprotein,purification,light quality, | en |
| dc.relation.page | 70 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2010-08-18 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 漁業科學研究所 | zh_TW |
| 顯示於系所單位： | 漁業科學研究所 | |
文件中的檔案：
| 檔案 | 大小 | 格式 | |
|---|---|---|---|
| ntu-99-1.pdf 未授權公開取用 | 5.19 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。