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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | 陳逸夫 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:16:57Z | - |
| dc.date.available | 2021-07-01T08:16:57Z | - |
| dc.date.issued | 1993 | |
| dc.identifier.citation | Banaszak, L.J., and Bradshaw, R.A. 1975. Malate dehydrogenase, in: P.D. Boyer (ed.), The Enzymes, Vol. XI, Academic Press, New York, San Francisco, London, pp. 369-396. Beasley, R.P., and Hwang, L.-Y. 1984. Epidemiology of hepatocellular carcinoma, in G.N. Vyas, J.L. Dienstag, and J.F. Hoofuagle (ed.), Viral hepatitis and liver disease. Grune and Stratton, Inc., Orlando, Fla. p.209-224. Bergmeyer, H.U., and Bernt, E. 1974 Malate dehydrogenase, in: H.U. Bergmeyer (ed.), Method of Enzymatic Analysis, Vol.2, 2nd. English ed., Verlag chemie Weinheim/Academic Press, New York, pp. 613-617. Brown, S.E., Stanley, C., Howard, C.R., Zuckerman, A.J., and Steward, M.W. 1986. Antibody responses to recombinant and plasma derived hepatitis B vaccines. Br. Med. J. 292: 159-161. Cattaneo, R.O., Will, H., and Schaller, H. 1984. Hepatitis B virus transcription in the infected liver. J. Embo. 3: 2191-2196. Cattaneo, R.O., Will, H., Hernandez, N., and Schaller, H. 1983. Signals regulating hepatitis B surface antigen transcription. Nature (London) 305:336-338. Cheng, K.-C., and Moss, B. 1987. Selective synthesis and secretion of particles composed of the hepatitis B middle surface protein directed by a recombinant vaccinia virus: Induction of antibodies to pre-S and S epitopes. J. Virol. 61:1286-1290. Cheng, K-C., Smith, G.L., and Moss, B. 1986. Hepatitis B virus large surface protein is not secreted but is immunogenic when selectively expressed by recombinant vaccinia virus. J. Virol. 60:337-344. Dixon, M., and Webb, E.C. Enzymes, Academic Press, New York 1958. Eble, B.E., Lingappa, V.R., and Ganem, D. 1986. Hepatitis B surface antigen: an unusual secreted protein initially synthesized as a transmembrane polypeptide. Mol. Cell. Biol. 6:1454-1463. Fraser, M.J. 1989. In Vitro Cell. Devel. Biol. 25:225-235. Ganem, D., and Varmus, H.E. 1987. The molecular biology of the hepatitis B viruses. Annu. Rev. Biochem. 56:651-695. Gough, N.M. 1983. Core and e antigen synthesis in rodent cells transformed with hepatitis B virus DNA is associated with greater than genome length viral messenger RNAs. J. Mol. Biol. 165:683-699. Heermann, K.H., Goldman U., Schwartz, W., Seyffarth, T., Baumgarten, H., and Gerlich, W.H. 1984. Large surface proteins of hepatitis B virus containing the pre-S sequence. J. Virol. 50:396-402. Jarvis, D.L., and Summers, M.D. 1989. Glycosylation and secretion of tissue plasminogen activator in recombinant baculovirus-infected insect cells. Mol. Cell. Biol. 9:214-223. Jilg, W., Schmidt, M., Zoulek, G., Lorbeer, B., Wilske, B., and Deinhardt, F. 1984. Lancet II, 1174-1175. Kang, C.Y., Bishop, D.H.L., Seo, J.-S., Matsuura, Y., and Choe, M. 1987. Secretion of particles of hepatitis B surface antigen from insect cells using a baculovirus vector. J.Gen.Virol. 68:2607-2613. Kelly, D.C., and Wang, X. 1981. Ann. Virol. (Inst.Pasteur), 132E, 247-259. King, J. 1965. Malate dehydrogenase, Practical Clinical Enzymology, Van Nostrand London, pp.93-99. Kitts, P.A., Ayres, M.D., and Possee, R.D. 1990. Linearization of baculovirus DNA enhances the recovery of recombinant virus expression vectors. Nucleic Acids Res. 18:5667-5672. Lanford, RE., Luckow, V.A., Kennedy, R.C., Dreesman, G.R., Notvall, L., and Summers, M.D. 1989. Expression and characterization of hepatitis B virus surface antigen polypeptides in insect cells with a baculovirus expression system. J. Virol. 63:1549-1557. Luckow, V.A., and Summers, M.D. 1988a. Signals important for high-level expression of foreign genes in Autographa californica nuclear polyhedrosis virus expression vectors. Virology 167:56-71. Luckow, V.A., and Summers, M.D. 1988b. Trends in the development of baculovirus expression vectors. Bio/Technology 6:47-55. Machida, A., Kishimoto, S., Ohumura, H., Miyamoto, K., Baba, K., Nakamura, T., and Miyakawa, Y. 1983. A hepatitis B surface antigen polypeptide (p31) with the receptor for polymerized human as well as chimpanzee albumins. Gastroenterology 85:268-274. Maeda, S., Kawai, T., Obinata, M., Fujiwara, H., Horiuchi, T., Saeki, Y., Sato, Y., and Furusawa, M. 1985. Production of human α-interferon in silkworm using a baculovirus vector. Nature 315:592-594. Machida, A., Kishimoto, S., Ohnuma, H., Baba, K., Ito, Y., Miyamoto, H., Funatsu, G., Oda, K., Usuda, S., Togami, S., Nakamura, T., Miyakawa, Y., and Muyumi, M. 1984. A polypeptide containing 55 amino acid residues coded by the pre-s region of hepatitis B virus deoxyribonucleic acid bears the receptor for polymerized human as well as chimpanzee albumins. Gastroenterology 86:910-918. Mclachlan, A., Milich, D.R., Raney, A.K., Riggs, M.G., Hughes, J.L., Sorge, J., and Chisari, F.V. 1987. Expression of hepatitis B virus surface and core antigens: Influence of the pre-S and precore sequences. J.Virol. 51:683-692. Milich, D.R., Thornton, G.B., Neurath, A., Kent, S., Michel, M., Tiollais, P., and Chisari, F.V. 1985. Enhanced immunogenicity of the pre-S region of hepatitis B surface antigen. Science 228:1195-1199. Milich, D.R., Mclachlan, A., Chisari, F.V., Kent, S.B.H., and Thornton, G.B. 1986. Immune response to the pre-S(1) region of the hepatitis B surface antigen (HBsAg): A pre-S(1) Specific T cell response can bypass nonresponsiveness to the pre-S(2) and S regions of HBsAg. J. Immunol. 137:315-322. Miller, D.W., Safer, P., and Miller, L.K. 1986. In Setlow, J.K., and Hollaender, A. (eds), Genetic Engineering.Plenum, New York, Vol. 8:277-298. Molnar-Kimber, K.L., arocki-Witek, V., Dheer, S.K., Vernon, S.K., Conley, A.J., Davis, A.R., and Hung, P.P. 1988. Distinctive properties of the hepatitis B virus envelope proteins. J. Virol. 62:407-416. Neurath, A.R., Kent, S.B.H., Strick, N., Taylor, P., and Stevens, C.E. 1984. Hepatitis B virus contains pre-s gene-encoded domains. Nature (London) 315:154-156. Neurath, A.R., Kent, S., Strick, N., and Parker, K. 1986. Identification and chemical systhesis of a host cell receptor binding site on hepatitis B virus. Cell 46:429-436. Neurath, A.R., Kent, S., and Strick, N. 1984. Location and chemical synthesis of a preS gene coded immunodominant epitope of hepatitis B virus. Science 224:392-395. Persing, D.H., Varmus, H.E., and Ganem, D. 1986. Inhibition of secretion of hepatitis B surface antigen by a related presurface polypeptide. Science 234:1388-1391. O'Reilly, D.R., Miller, L.K., and Luckow, V.A. 1992. Baculovirus expression vectors: a laboratory manual. Persing, D.H., Varmus, H.E., and Ganem, D. 1985. A frameshift mutation in the pre-S region of the human hepatitis B virus genome allows production of surface antigen particles but eliminates binding to polymerized albumin. Proc.Natl.Acad.Sci.USA 82:3440-3444. Peterson, D., Roberts, I., and Vyas, G. 1977. Partial amino acid sequence of two major component polypeptides of hepatitis B surface antigen. Proc.Natl. Acad.Sci.USA 74:1530-1534 Possee, R.D., and Kitts, P.A. 1993. A method for producing recombinant baculovirus expression vectors at high frequency. BioTechniques (in press) Price, P.M., Mohamad, A., Zelent, A., Neurath, A.R., and Acs, G. 1988. Translational selection in the expression of the hepatitis B virus envelope proteins. DNA 7:417-422. Scully, L.J., and Kang, C.Y. 1988. Production and secretion of hepatitis B surface antigen (HBsAg) and Pre-S2 plus HBsAg using a baculovirus expression vector. Viral Hepatitis and Liver Disease. pp.365-371. Shen, W.-C., Mauck, L., and Colman, R.F. 1974. Physicochemical properties of the diphosphopyridine nucleotide-specific isocitrate dehydrogenase of pig heart. J.Biol.Chem. 249:7942-7949. Smith, G.E., Summers, M.D., and Fraser, M.J. 1983b. Production of human β-interferon in insect cells infected with a baculovirus expression vector. Mol.Cell.Biol.3: 2156-2165. Standring, D.N., Rutter, W.J., Varmus, H.E., and Ganem, D. 1984. Transcription of the hepatitis B virus surface antigen gene in cultured murine cells initiates within the presurface region. J.Virol. 50:563-571. Standring, D.N., Ou, J.-H., and Rutter, W.J. 1986. Assembly of viral particles in Xenopus oocytes: pre-surface antigens regulate secretion of the hepatitis B viral surface envelope particle. Proc.Natl.Acad.Sci.USA 83:9338-9342. Stevens, C.E., Taylor, P.E., Tong, M.J., Toy, P.T., and Vyas, G.N. 1984. in Viral Hepatitis and Liver Disease, eds. Vyas, G.N., Dienstag, J.L., and Hoofnagle, J.H. (Grune and Stratton, Orlando, FL), pp.275-291. Stibbe, W., and Gerlich, W.H. 1983. Structural relationships between minor and major proteins of hepatitis B surface antigen. J.Virol. 46:626-628. Tiollais, P., Pourcel, C., and Dejean, D. 1985. The hepatitis B virus. Nature 317:489-495. Vialard, J., Lalumiere, M., Vernet, T., Briedis, D., Alkhatib, G., Henning, D., Levin, D., and Richardson, C. 1990. Synthesis of the membrane fusion and hemagglutinin proteins of measles virus, using a novel baculovirus vector containing the β-galactosidase gene. J. Virol. 64:37-50. Vlak, J.M., and Smith, G.E. 1982. Orientation of the genome of Autographa californica nuclear polyhedrosis virus:a proposal. J. Virol. 41:1118-1121. Vlak, J.M., Schouten, A., Usmany, M., Belsham, G.J., Klinge-Roode, E.C., Maule, A.J., van Lent, J.W.M., and Zuidema, D. 1990. Expression of cauliflower mosaic virus gene I using a baculovirus vector based upon the p10 gene and a novel selection method. Virology 179:312-320. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75980 | - |
| dc.description.abstract | 以市售桿狀病毒轉形試劑組所得之重組病毒比例,並非如預期的接近百分之百,因此擬得純系化之重組病毒及較高之重組蛋白產量,至少須經兩次以上病毒純化。接著,取純化過並載有B型肝炎表面抗原M protein基因之重組病毒,與兩株僅載有S protein基因之重組病毒分別感染昆蟲細胞,發現S protein幾乎不分泌至培養液,絕大部分累積在細胞內;反觀在感染後四十八小時即於培養液中偵測到相當量之分泌性M protein。此外,當昆蟲細胞中同時存在M與S protein時,M protein將有抑制S protein分泌之可能。 | zh_TW |
| dc.description.abstract | The fraction of recombinant virus which was obtained from cotransfection fluids using commercial transfection kit was not nearly 100% as expected.So purified recombinants and higher recombinant protein production could only be approached when undergone virus purification twice.Then we analyzed the secretion of HBV M and S proteins from three recombinant viruses containing either M or S protein gene. The results indicated that the S proteins were predominantly accumulated in the insect cells and were inefficiently secreted into the medium.In contrast, there were comparatively high level of the M proteins in the medium two days after infection.On the other hand, the secretion of the S proteins were presumably inhibited by the presence of the M proteins. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:16:57Z (GMT). No. of bitstreams: 0 Previous issue date: 1993 | en |
| dc.description.tableofcontents | 壹、緒言……………………………………1 一、桿狀病毒表現載體系統……………………………………1 二、B型肝炎表面抗原之基因結構、功能與分泌作用……………………………………4 三、本論文研究主題……………………………………7 貳、材料與方法……………………………………9 材料……………………………………9 方法……………………………………10 一、重組病毒之純化……………………………………10 二、分析病毒純化對重組蛋白產量之影響……………………………………11 三、以酵素免疫分析法(EIA)測定三株重組病毒細胞內外HBsAg產量……………………………………11 四、三種去氫酵素活性之測定……………………………………12 a.Malate dehydrogenase……………………………………12 b.Lactate dehydrogenase……………………………………13 c.Isocitrate dehydrogenase……………………………………14 五、以免疫沉澱法(immunoprecipitation)分析細胞內外HBsAg產量……………………………………14 參、結果……………………………………16 一、重組病毒之純化……………………………………16 二、病毒純化對重組蛋白產量之影響……………………………………19 三、三株不同重組病毒HBsAg分泌型態之比較……………………………………25 四、以三種去氫酵素分析細胞溶裂變化與B型肝炎表面抗原分泌作用之關係……………………………………29 五、分泌性HBsAg組成之分析……………………………………37 肆、討論……………………………………41 伍、附錄……………………………………49 陸、英文摘要……………………………………53 柒、中文摘要……………………………………54 捌、參考文獻……………………………………55 | |
| dc.language.iso | zh-TW | |
| dc.title | 利用桿狀病毒載體系統研究在昆蟲細胞中B型肝炎表面抗原之合成與分泌作用 | zh_TW |
| dc.title | Synthesis and Secretion of Hepatitis B Surface Antigen (HBsAg) in Insect Cells Using Baculovirus Expression Vectors | en |
| dc.date.schoolyear | 81-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 65 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 動物學研究所 | zh_TW |
| 顯示於系所單位: | 動物學研究所 | |
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