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DC 欄位 | 值 | 語言 |
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dc.contributor.author | 朱蔡豈 | zh_TW |
dc.date.accessioned | 2021-07-01T08:19:56Z | - |
dc.date.available | 2021-07-01T08:19:56Z | - |
dc.date.issued | 1997 | |
dc.identifier.citation | Abrieu, A., Lorca, T., Labbe', J.- C., Morin, N., Keyse, S. & Dore'e, M. (1996). MAP kinase does not inactivate, but rather prevents the cyclin degradation pathway from being turned on in Xenopus egg extracts. J. Cell Sci. 109, 239-246. Braford, M. M. (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. Chen, M., Li, D., Krebs, E. G. & Cooper, J. A. (1997). The casein kinase II β subunit binds to Mos and inhibits Mos activity. Mol. Cell. Biol. 17, 1904-1912. Choi, T., Aoki, F., Mori, M., Yamashita, M., Nagahama, Y., & Kohmoto, K. (1991). Activation of p34cdc2 protein kinase activity in meiotic and mitotic cell cycles in mouse oocytes and embryos. Development 113, 789-795 Colgan, D. F., Murthy, K. G. K., Prives, C., & Manley, J. L. (1996). Cell-cycle related regulation of poly(A) polymerase by phosphorylation. Nature 384, 282-285. Colledge, W. H., Carlton, M. B. L., Udy, G. B. & Evans, M. J. (1994). Disruption of c-mos causes parthenogenetic development of unfertilized mouse eggs. Nature 370, 65-68. Cyert, M. S. & Kirschner, M. (1988). Regulation of MPF activity in vitro. Cell 53, 185-195. Frankel, A. E. & Fischinger, P. J. (1976). Nucleotide sequences in mouse DNA and RNA specific for Moloney sarcoma virus. Proc. Natl. Acad. Sci. USA 73, 3705-3709. Freeman, R. S., Ballantyne, S. M. & Donoghue, D. J. (1991). Meiotic induction by Xenopus cyclin B is accelerated by coexpression with mosxe. Mol. Cell. Biol. 11, 1713-1717. Freeman, R. S., Meyer, A. N., Li, J. & Donoghue, D. J. (1992). Phosphorylation of conserved serine residues does not regulate the ability of mosxe protein kinase to induce oocyte maturation or function as cytostatic factor. J. Cell Biol. 116, 725-735. Furuno, N., Nishizawa, M., Okazaki, K., Tanaka, H., Iwashita, J., Nakajo, N., Ogawa, Y. & Sagata, N. (1994). Suppression of DNA replication via Mos function during meiotic divisions in Xenopus oocytes. EMBO J. 13, 2399-2410. Gabrielli, B. G., Roy, L. M. & Maller, J. L. (1993). Requirement for Cdk2 in cytostatic factor-mediated metaphase II arrest. Science 259, 1766-1769. Gavin, A. C., Cavadore, J. C., & Schorderet S. S. (1994) Histone Hl kinase activity, germinal vesicle breakdown and M phase entry in mouse oocytes. J. Cell Sci. 107, 275-283 Gebauer, F. & Richter, J. D. (1997). Synthesis and function of Mos: the control switch of vertebrate oocyte meiosis. BioEssays 19, 23-28. Gebauer, F., Xu, W., Cooper, G. M. & Richter, J. D. (1994). Translational control by cytoplasmic polyadenylation of c-mos mRNA is necessary for oocyte maturation in the mouse. EMBO J. 13, 5712-5720. Goldman, D. S., Kiessling, A. A., Millette, C. F. & Cooper, G. M. (1987). Expression of c-mos RNA in germ cells of male and female mice. Proc. Natl. Acad. Sci. USA 84, 4509-4513. Gotoh, Y., Masuyama, N., Dell, K., Shirakabe, K. & Nishida, E. (1995). Initiation of Xenopus oocyte maturation by activation of the mitogen-activated protein kinase cascade. J. Biol. Chem. 270, 25898-25904. Haccard, O., Sarcevic, B., Lewellyn, A., Hartley, R., Roy, L., Izumi, T., Erikson, E. & Maller, J. L. (1993). Induction of metaphase arrest in cleaving Xenopus embryos by MAP kinase. Science 262, 1262-1265. Hake, L. E. & Richter, J. D. (1994). CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell 79, 617-627. Hanks, S. K., Quinn, A. M. & Hunter, T. (1988). The protein kinase family: features and deduced phylogeny of the catalytic domains. Science 241, 42-52. Harlow, E. & Lane, D. (1988). Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory press, USA. Hashimoto, N., Watanabe, N., Furuta, Y., Tamemoto, H., Sagata, N., Yokoyama, M., Okazaki, K., Nagayoshi, M., Takeda, N., Ikawa, Y. & Aizawa, S. (1994). Parthenogenetic activation of oocytes in c-mos-deficient mice. Nature 370, 68-71. Johnson, L. N., Noble, M. E. M. & Owen, D. J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158. Jung, T., Moor, R. M., & Fulka, J. J. (1993) Kinetics of MPF and histone kinase activity differ during the G2-to M-phase transition in mouse oocytes. Int. J Dev. Biol. 37, 595-600 Kanki, J. P. & Donoghue, D. J. (1991). Progression from meiosis I to meiosis II in Xenopus oocytes requires de novo translation of the mosxe protooncogene. Proc. Natl. Acad. Sci. USA 88, 5794-5798. Kajiura, H., Yamashita, M., Katsu, Y. & Nagahama, Y. (1993). Isolation and characterization of cdc2, a catalytic component of maturation-promoting factor. Dev. Growth Diff. 35, 647-654. Katsu, Y., Yamashita, M., Kajiura, H. & Nagahama, Y. (1993). Behavior of components of maturation-promoting factor, cdc2 kinase and cyclin B, during oocyte maturation of goldfish. Dev. Biol. 160, 99-107. King, R. W., Deshaies, R. J., Peters, J.- M. & Kirschner, M. W. (1996). How proteolysis drives the cell cycle. Science 274, 1652-1659. Kleckner, N. (1996). Meiosis: how could it work Proc. Natl. Aca. Sci. USA 93, 8167-8174. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. Leibovitch, S. A., Lenormand, J. L., Leibovitch, M. P., Guiller, M., Mallard, L., and Harel, J. (1990). Rat myogenic c-mos cDNA: cloning sequence analysis and regulation during muscle development. Oncogene 5, 1149-1157. Lorca, T., Cruzalegui, F. H., Fesquet, D., Cavadore, J.- C., Me'ry, J., Means, A. & Dore'e, M. (1993). Calmodulin-dependent protein kinase II mediates inactivation of MPF and CSF upon fertilization of Xenopus eggs. Nature 366, 270-274. Lorca, T., Galas, S., Fesquet, D., Devault, A., Cavadore, J.- C. & Dore'e, M. (1991). Degradation of the proto-oncogene product p39mos is not necessary for cyclin proteolysis and exit from meiotic meiotic metaphase: requirement for a Ca2+-calmodulin dependent event. EMBO J. 10, 2087-2093. Lu, K. P. & Hunter T. (1995) Evidence for a NIMA-like mitotic pathway in vertebrate cells. Cell 81, 413-424. Maller, J., Wu, M. & Gerhart, J. C. (1977). Changes in protein phosphorylation accompanying maturation of Xenopus laevis oocytes. Dev. Biol. 58, 295-312. Marshall, C. J. (1994). Hot lips and phosphorylation of protein kinase. Nature 367, 686. Masui, Y. & Markert, C. L. (1971). Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177, 129-146. Matten, W. T., Copeland, T. D., Ahn, N. G. & Vande Woude, G. F. (1996). Positive feedback between MAP kinase and Mos during Xenopus oocyte maturation. Dev. Biol. 179, 485-492. Maxwell, S. A. & Arlinghaus, R. B. (1985a). Use of site-specific antipeptide antibodies to perturb the serine kinase catalytic activity of p37mos. J. Virol. 55, 874-876. Maxwell, S. A. & Arlinghaus, R. B. (1985b). Serine kinase activity associated with Moloney murine sarcoma virus-124-encoded p37mos. Virology 143, 321-333. McGrew, L. L. & Richter, J. D. (1990). Translational control by cytoplasmic polyadenylation during Xenopus oocyte maturation: characterization of cis and trans elements and regulation by cyclin/MPF. EMBO J. 9, 3743-3751. Minshull, J., Sun, H., Tonks, N. K. & Murray, A. W. (1994). A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts. Cell 79, 475-486. Mirai, T., Yamashita, M., Yoshikuni, M., Lou, Y. H. & Nagahama, Y. (1992). Cyclin B in fish oocytes: its cDNA and amino acid sequences, appearance during maturation, and induction of p34-cdc2 activation. Mol. Reprod. Dev. 33, 131-140. Murray, A. & Hunt, T. (1993). The Cell Cycle: An Introduction. Oxford University press, New York. Murray, A. W. (1992). Creative blocks: cell-cycle checkpoint and feedback controls. Nature 359, 599-604. Mutter, G. L. & Wolgemuth, D. J. (1987). Distinct developmental patterns of c-mos proto-oncogene expression in female and male mouse germ cells. Proc. Natl. Acad. Sci. USA 84, 5301-5305. Nasmyth, K. (1996). Viewpoint: putting the cell cycle in order. Science 274, 1643-1646. Nebreda, A. R. & Hunt, T. (1993). The c-mos proto-oncogene protein kinase turns on and maintains the activity of MAP kinase, but not MPF, in cell-free extracts of Xenopus oocytes and eggs. EMBO J. 12, 1979-1986. Nishizawa, M., Furuno, N., Okazaki, K., Tanaka, H., Ogawa, Y. & Sagata, N. (1993). Degradation of Mos by the N-terminal proline (Pro2)-dependent ubiquitin pathway on fertilization of Xenopus eggs: possible significance of nature selection for Pro2 in Mos. EMBO J. 12, 4021-4027. Nishizawa, M., Okazaki, K., Furuno, N., Watanabe, N. & Sagata, N. (1992). The second codon rule and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes. EMBO J. 11, 2433-2446. O'Keefe, S. J., Kiessling, A. A. & Cooper, G. M. (1991). The c-mos gene product is required for cyclin B accumulation during meiosis of mouse eggs. Proc. Natl. Acad. Sci. USA 88, 7869-7872. O'Keefe, S. J., Wolfes, H., Kiessling, A. A. & Cooper, G. M. (1989). Microinjection of antisense c-mos oligonucleotides prevents meiosis II in the maturing mouse egg. Proc. Natl. Acad. Sci. USA 86, 7038-7042. Oskarsson, M., McClements, W. L., Blair, D. G., Maizel, J. V. & Vande Woude, G. F. (1980). Properties of a normal mouse cell DNA sequence (sarc) homologous to the src sequence of Moloney sarcoma virus. Science 207, 1222-1224. Paules, R. S., Buccione, R., Moschel, R. C., Vande Woude, G. F. & Eppig, J. J. (1989). Mouse mos protooncogene product is present and functions during oogenesis. Proc. Natl. Acad. Sci. USA 86, 5395-5399. Paules, R. S., Propst, F., Dunn, K. J., Blair, D. G., Kaul, K., Palmer, A. E. & Vande Woude, G. F. (1988). Primate c-mos proto-oncogene and expression: transcription initiation both upstream and within the gene in a tissue-specific manner. Oncogene 3, 59-68. Pickham, K. M., Meyer, A. N., Li, J. & Donoghue, D. J. (1992). Requirement of mosxe protein kinase for meiotic maturation of Xenopus oocytes induced by a cdc2 mutant lacking regulatory phosphorylation sites. Mol. Cell. Biol. 12, 3192-3203. Pomerance, M., Thang, M. N., Tocque, B. & Pierre, M. (1996). The Ras-GTPase-activating protein SH3 domain is required for cdc2 activation and mos induction by oncogenic Ras in Xenopus oocytes independently of mitogen-activated protein kinase activation. Mol. Cell. Biol. 16, 3179-3186. Posada, J. & Cooper, J. A. (1992). Requirements for phosphorylation of MAP kinase during meiosis in Xenopus oocytes. Science 255, 212-215. Posada, J., Yew, N., Ahn, N. G., Vande Woude, G. F. & Cooper, J. A. (1993). Mos stimulates MAP kinase in Xenopus oocytes and activates a MAP kinase kinase in vitro. Mol. Cell. Biol. 13, 2546-2553. Roy, L. M., Singh, B., Gautier, J., Arlinghaus, R. B., Nordeen, S. K. & Maller, J. L. (1990). The cyclin B2 component of MPF is a substrate for the c-mosxe proto-oncogene product. Cell 61, 825-831. Roy, L. M., Haccard, O., Izumi, T., Lattes, B. G., Lewellyn, A. L. & Maller, J. L. (1996). mos proto-oncogene function during oocyte maturation in Xenopus. Oncogene 12, 2203-2211. Sagata, N. (1996). Meiotic metaphase arrest in animal oocytes: its mechanisms and biological significance. Trends Cell Biol. 6, 22-28. Sagata, N. (1997). What does Mos do in oocytes and somatic cells BioEssays 19, 13-21. Sagata, N., Daar, I., Oskarsson, M., Showalter, S. D. & Vande Woude, G. F. (1989a). The product of the mos proto-oncogene as a candidate initiator for oocyte maturation. Science 245, 643-646. Sagata, N., Oskarsson, M., Copeland, T., Brumbaugh, J. & Vande Woude, G. F. (1988). Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature 335, 519-525. Sagata, N., Watanabe, N., Vande Woude, G. F. & Ikawa, Y. (1989b). The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 342, 512-518. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular cloning: A Laboratory Manual. 2nd ed. Cold Spring Harbor Laboratory press, USA. Schein, C. H. (1989). Production of soluble recombinant proteins in bacteria. Bio/Technology 7, 1141-1147. Schmidt, M., Oskarsson, M., Dunn, J. K., Blair, D. G., Hughes, S., Propst, F. & Vande Woude, G. F. (1988). Chicken homolog of the mos proto-oncogene. Mol. Cell. Biol. 8, 923-929. Schweitzer, B. & Philippsen, P. (1991). Cdc15, an essential cell cycle gene in Saccharomyces, encodes a protein kinase domain. Yeast 7, 265-274. Seth, A. & Vande Woude, G. F. (1985). Nucleotide sequence and biochemical activities of the Moloney murine sarcoma virus strain HT-1 mos gene. J. Virol. 56, 144-152. Seth, A., Priel, E. & Vande Woude, G. F. (1987). Nucleoside triphosphate-dependent DNA-binding properties of mos protein. Proc. Natl. Acad. Sci. USA 84, 3560-3564. Sheets, M. D., Fox, C. A., Hunt, T., Vande Woude, G. & Wickens, M. (1994). The 3'untranslated regions of c-mos and cyclin mRNAs stimulate translation by regulating cytoplasmic polyadenylation. Genes Dev. 8, 926-938. Sheets, M. D., Wu, M. & Wickens, M. (1995). Polyadenylation of c-mos mRNA as a control point of Xenopus meiotic maturation. Nature 374, 511-516. Shibuya, E. K. & Masui, Y. (1988). Stabilization and enhancement of primary cytostatic factor (CSF) by ATP and NaF in amphibian egg cytosols. Dev. Biol. 129, 253-264. Singh, B., Herzog, N. K., Liu, J. & Arlinghaus, R. B. p37mos encoded by HT-1 strain of Moloney murine sarcoma virus has an associated protein kinase activity. Oncogene 3, 79-85. Stader, J. A. & Silhavy T. J. (1990). Engineering Escherchia coli to secrete heterologous gene products. Meth. Enzymol. 185, 166-195 Stebbins-Boaz, B., Hake, L. E. & Richter, J. D. (1996). CPEB controls the cytoplasmic polyadenylation of cyclin, Cdk2 and c-mos mRNAs and is necessary for oocyte maturation in Xenopus. EMBO J. 15, 2582-2592. Stillman, B. (1996). Cell cycle control of DNA replication. Science 274, 1659-1664. Van Beveren, C., van Straaten, F., Galleshaw, J. A. & Verma, I. M. (1981). Nucleotide sequence of the genome of a murine sarcoma virus. Cell 27, 97-108. Vander Hoorn, F. A. & Firzlaff, J. (1984). Complete c-mos (rat) nucleotide sequence: presence of conserved domains in c-mos proteins. Nucleic Acids Res. 12, 2147-2156. Vande Woude, G. F. & Propst, F. (1985). Expression of c-mos proto-oncogene transcripts in mouse tissues. Nature 315, 516-518. Verlhac, M.- H., Kubiak, J. Z., Weber, M., Ge'raud, G., Colledge, W. H., Evans, M. J. & Maro, B. (1996). Mos is required for MAP kinase activation and is involved in microtubule organization during meiotic maturation in the mouse. Development 122, 815-822. Wallace R. B. & Selman K. (1990) Ultrastructural aspects of oogenesis and oocyte growth in fish and amphibians. J. Elec. Microsc. Tech. 16, 175-201. Wang, X. M., Yew, N., Peloquin, J. G., Vande Woude, G. F. & Borisy, G. G. (1994). Mos oncogene product associates with kinetochores in mammalian somatic cells and disrupts mitotic progression. Proc. Natl. Acad. Sci. USA 91, 8329-8333. Watanabe, N., Hunt, T., Ikawa, Y. & Sagata, N. (1991). Independent inactivation of MPF and cytostatic factor (Mos) upon fertilization of Xenopus eggs. Nature 352, 247-248. Watanabe, N., Vande Woude, G. F., Ikawa, Y. & Sagata, N. (1989). Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs. Nature 342, 505-511. Watson, R., Oskarsson, M. & Vande Woude, G. F. (1982). Human DNA sequence homologous to the transforming gene (mos) of Moloney murine sarcoma virus. Proc. Natl. Acad. Sci. USA 79, 4078-4082. Wickner W., Driessen J. M. & Hartl F.-U (1991). The enzymology of protein translocation across the Escherichia coli plasma membrane. Annu. Rev. Biochem. 60, 101-124. Wormington, M. (1993). Poly(A) and translation: development control. Curr. Opin. Cell Biol. 5, 950-954. Xu, W., Ladner, K. J. & Smith, L. D. (1992). Evidence that Mos protein may not act directly on cyclin. Proc. Natl. Acad. Sci. USA 89, 4573-4577. Yamashita, M., Fukada, S., Yoshikuni, M., Bulet, P., Hirai, T., Yamaguchi, A., Lou, Y.- H., Zhao, Z. & Nagahama, Y. (1992). Purification and characterization of maturation-promoting factor in fish. Dev. Biol. 149, 8-15. Yamashita, M., Kajiura, H., Tanaka, T., Onoe, S. & Nagahama, Y. (1995). Molecular mechanism of the activation of maturation-promoting factor during goldfish oocyte maturation. Dev. Biol. 168, 62-75. Yew, N., Mellini, M. L. & Vande Woude, G. F. (1992). Meiotic initiation by the mos protein in Xenopus. Nature 355, 649-652. Zhou, R., Oskarsson, M., Paules, R. S., Schulz, N., Cleveland, D. & Vande Woude, G. F. (1991). Ability of the c-mos product to associate with and phosphorylate tubulin. Science 251, 671-675. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76291 | - |
dc.description.abstract | c-mos基因產物是個蛋白激?,在脊椎動物之卵成熟過程中調節各項重要事件。就蛙卵而言,Mos蛋白激?負責誘發GVBD(germinal vesicle breakdown),於第一次和第二次減數分裂過渡時抑制DNA合成,並維持成熟卵靜止於第二次減數分裂中期。Mos蛋白激?之作用機制與MPF(maturation-promoting factor)作用有著密不可分之關係,與Mos蛋白質交互作用之分子更結合成一複雜之交織。此多元化之分子性質,可能歸因於Mos蛋白質合成初期不穩定之性質與磷酸化狀態而達成。對於Mos蛋白之生理研究,多採融合蛋白進行研究。鯉魚卵成熟樣態與蛙卵系統有所不同,但鯉魚卵成熟之研究僅止於MPF,尚缺乏完整分子機制之構圖。本實驗室則用已選殖到的鯉魚c-mos基因,利用分子生物技術,促使細菌表現c-mos非融合蛋白,以極溫和之純化步驟獲取較近於內生性之Mos蛋白,並針對此蛋白作了一些基本性狀探討及與魚卵萃液之蛋白質之交互作用。發現到表現的Mos蛋白在純化後去鹽時有消失的現象。並且發現到細菌表現蛋白為—磷酸蛋白,且於表現之初便已呈磷酸化狀態。這些基本性狀及初步於卵萃液中之觀察對於未來c-mos蛋白在魚卵成熟分子機制的研究將會有所助益。 | zh_TW |
dc.description.abstract | The Mos protein kinase, product of the c-mos proto-oncogene, is a key regulator of oocyte maturation in vertebrates. In Xenopus laevis, Mos protein kinase is involved in inducing germinal vesicle breakdown, inhibiting DNA replication during meiosis I/meiosis II transition and maintaining the metaphase arrest of meiosis II in mature eggs. Maturation promoting factor (MPF) activities during oocyte maturation are also regulated by Mos or Mos-mediated mechanisms. Mos also interacts with many molecules other than MPF. The multi-functional properties of Mos might be attributed to its various phosphorylation states and instable property. In spite of the apparent conformation problems, most researches in Xenopus oocyte system used Mos fusion protein as a tool. On the other hand, researches in fish oocyte maturation are in relatively slow progression without incorporating Mos into studies. We had cloned c-mos gene from the carp genomic library. In this study, the c-mos gene product of the carp was expressed as a non-fusion protein in E. coli. The expressed protein showed different characters from Mos fusion protein utilized in the study of Xenopus oocytes. Caracterization of the carp c-mos protein in vitro will help the investigation of Mos molecular mechanism in vivo in the future. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:19:56Z (GMT). No. of bitstreams: 0 Previous issue date: 1997 | en |
dc.description.tableofcontents | 中文摘要………………………………………………………………………Ⅰ 英文摘要………………………………………………………………………Ⅱ 序言 一.減數分裂是卵形成的必經過程…………………………………………1 二.c-mos蛋白激?是卵成熟過程中重要的調節分子……………………1 三.Mos蛋白質合成顯現母源mRNA典型的轉譯調節機制…………………3 四.Mos在卵子成熟過程中調節減數分裂進展之分子機制………………8 五.Mos蛋白質在卵細胞中消解的機制……………………………………14 六.鯉魚卵成熟過程中減數分裂進程之分子機制………………………16 材料與方法 一.鯉魚c-mos基因coding region之選殖與表現………………………18 二.以表現蛋白製造抗血清………………………………………………21 三.大量表現B-Moscarp及純化……………………………………………22 四.B-Moscarp穩定度之觀察………………………………………………24 五.B-Moscarp及魚卵萃取液之免疫偵測…………………………………25 六.鯉魚卵萃取液之製備及觀察…………………………………………26 結果 一.構築表現載體並確認…………………………………………………28 二.生產可溶性且高純度之B-Moscarp……………………………………29 三.B-Moscarp之不穩定性…………………………………………………30 四.B-Moscarp與魚卵萃液中蛋白質的交互作用…………………………31 五.魚卵萃取液中Mos蛋白質之偵測………………………………………32 六.細菌表現之B-Moscarp可能為—磷酸蛋白質…………………………32 討論 一.可溶性表現蛋白B-Moscarp之生產方式及應用………………………44 二.B-Moscarp不穩定性狀之探討…………………………………………45 三.找出與B-Moscarp交互作用之蛋白質…………………………………46 四.偵測鯉魚卵內c-mos基因產物…………………………………………47 五.B-Moscarp為磷酸蛋白質………………………………………………48 參考資料……………………………………………………………………49 | |
dc.language.iso | zh-TW | |
dc.title | 鯉魚c-mos基因表現蛋白性狀及功能之探討 | zh_TW |
dc.title | Characterization and Functional Study on Expressed Protein of Carp c-mos Gene | en |
dc.date.schoolyear | 85-2 | |
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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