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DC 欄位 | 值 | 語言 |
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dc.contributor.author | 吳秋逸 | zh_TW |
dc.date.accessioned | 2021-07-01T08:11:24Z | - |
dc.date.available | 2021-07-01T08:11:24Z | - |
dc.date.issued | 1999 | |
dc.identifier.citation | A ?ali and T.L. Blundell. J. Mol. Biol 234,779-815, 1993. Atkinson, R.A., Saudek, V., and Pelton, J.T. Int. J. Pept. Protein Res. 43(6):563-572, 1994. Bauer, M., Sun, Y., Degenhardt, C., and Kozikowski, B. J. Protein Chem. 12(6):759-764, 1993. Betz, S.F. Protein Eng. 4,593-600, 1993. Bennett, J.S., Vilaire, G., and Cines, D.B. J. Biol. Chem. 257(14):8049-8054, 1982. Bernabei, A., Gikakis, N., Kowalska, M.A., Niewiarowski, S., and Edmunds, L.H., Ann. Thorac. Surg. 59(1):149-153, 1995. Bloch W., Forsberg E. J. Cell Biol. 139:265-278, 1997. Bouderau, N., Andrew C. J. Cell Biol. 139:257-264, 1997. Bronson, R.A., Gailit, J., Bronson, S., and Oula, L. Fertil. Steril. 64(2):414-420, 1995. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D.J., Swaminathan, S. and Karplus, M.J. Comp. Chem. 4:187-217, 1983 Brooks, P. C., Stromblad S., Sanders L. C. Cell 85: 683-693, 1996. Brooks, P. C., Stromblad S., Sanders L. C. J Clin. Invest. 96:1815-1822, 1995. Brooks, P.C., Montgomery M. P. Cell 79:1157-1164, 1994. Bujard, H., Gentz, R., Lanzer, M., Stueber, D., Mueller, M., Ibrahimi, I., Haeuptle, M.T., and Dobberstein, B. Methods Enzymol. 155:416-433, 1987. Calvete, J.J., McLane, M.A., Stewart, G.J. Biochem. Biophys. Res. Commun. 202(1):135-140, 1994. Capula, M. & Mazza, G. In Guide to Peptides and Amphibians of the World (Behler, J. L., Ed) 188, Slimon & Schuster, New York, 1989. Casimiro, D.R., Wright, P.E., and Dyson, H.J. Structure. 5(11):1407-1412, 1997. Chambers, A. F. and Matrisian J. Natl. Cancer Inst. 89:1260-1270, 1997. Chan, H. S., & Dill, K. A. J. Am. Chem. Soc. 112,6296-6303. 1990. Chen, Y., Pitzenberger, S.M., Garsky, V.M., Lumma, P.K., Sanyal, G., and Baum, J. Biochemistry 30(50):11625-11636, 1991. Chen, P-Y., S-H Wu, K-T Wang. Protein Eng. 7,941-944,1994a. Chen, Y., Sun, A.K., Kominos, D., Sanyal, G., Naylor, A.M., Pitzenberger, S.M., Garsky, V.M., Levy, R.M., and Baum, J. J. Biomol. NMR. 4(3):307-324, 1994b. Chen, Y-L, Huang, T.F., Chen, S. W., and Tsai, I.H. Biochem,. J. 305(Pt 2):513-520, 1995. Chia, Hsin Yeh, Hui-Chin Peng, and Tur-FU Huang Blood, 92:3268-3276, 1998. Chuang, L.C., Chen, P.Y., Chen, C., Huang, T.H., Wang, K.T., Chiou, S H. and Wu, S.H. Biochem. Biophys. Res. Commun. 220(2):246-254, 1996. Coller, B.S., Anderson, K., and Weisman, HF. Thromb. Haemost. 74(1):302-308, 1995. Cooke, R.M., Carter, B.G., Martin, D.M., Murray Rust, P., and Weir, M.P. Eur. J. Biochem. 202(2):323-328, 1991. Cooke, R.M., Carter, B.G., Murray Rust, P., Hartshorn, M.J., Herzyk, P., and Hubbard, R.E. Protein Eng. 5(6):473-477, 1992. Creigfton, T. E. J Mol. Biol. 87,563-577, 1974. Creigfton, T. E. J Mol. Biol. 113,275-293, 1977. Creighton, T. E. & Goldenberg, D. P. J. Mol. Biol. 17,497-526, 1984. Dadlez, M., & Kim, P. S. Nat. Struct. Biol. 2,674-679, 1995. Dalvit, C., Widmer, H., Bovermann, G., Breckenridge, R., and Metternich, R. Eur. J. Biochem. 202(2):315-321, 1991. Davie, E. W., and Ratmoff, O. D. Science 145:1310-1312, 1964 Davie, E. W., Fujikawa, K., Kisiel W. Biochemistry 30,10363-10370, 1991. Dennis, M.S., Henzel, W.J., Pitti, R.M., Lipari, M.T., Napier, M.A., Deisher, T A., Bunting, S., and Lazarus, R.A. Proc. Natl. Acad. Sci. U S.A. 87(7):2471-2475, 1990. Dresner Pollak, R. and Rosenblatt, M. J. Cell Biochem. 56(3):323-330, 1994. Du, P., Collins JR, Loew GH. Protein Eng. 5:679-691. 1992 Fider, I. J., and Ellis, L. M. Cell 79:185-188, 1994. Fisher, J.E., Caulfield, M.P., Sato, M., Quartuccio, H.A., Gould, R.J., Garsky, V.M., Rodan, G.A., and Rosenblatt, M. Endocrinology 132(3):1411-1413, 1993. Frelinger, A.L.,3d, Du, X.P., Plow, E.F., and Ginsberg, M.H. J. Biol. Chem. 266(26):17106-17111, 1991. G. Vriend. J. Mol. Graph. 8, 52-56, 1990. Gan, Z.R., Condra, J.H., Gould, R.J., Zivin, R.A., Bennett, C.D., Jacobs, J.W., Friedman, P.A., and Polokoff, M.A. Gene 79(1):159-166, 1989. Genetic Computer Group. Program Manual for the Wisconsin Package Science Drive Madison Wisconsin, USA 53711. Ghelvanayagam, G, Wilce. M. C. J, Parker. M. W, Tan. K. L, Board. P. G. Proteins. Structure, Function, and Genetics 27:118-130, 1997. Girma, J.P., Meyer, D., Verweij, C.L., Pannekoek, H., and Sixma, J.J. Blood 70(3):605-611, 1987. Gray, W.R. Protein Sci. 2(10):1749-1755, 1993. Grosjean, H. and Fiers, W. Gene 18(3):199-209, 1982. Grundstrom, T., Zenke, W.M., Wintzerith, M., Matthes, H.W., Staub, A., and Chambon, P. Nucleic. Acids. Res. 13(9):3305-3316, 1985. Hickey, M.J., Williams, S.A., and Roth, G.J. Proc. Natl. Acad. Sci. U.S.A. 86(17):6773-6777, 1989. Huang, T.F. and Ouyang, C. Thronib. Res. 33(2):125-138, 1984. Huang, T.F., Wu, Y.J., and Ouyang, C. Biochim. Biophys. Acta 925(3):248-257, 1987. Humphries, M.J. J. Cell Sci. 97(Pt 4):585-592, 1990. Hynes, R.O. Cell 48(4):549-554, 1987. Hynes, R.O. Cell 69(1):11-25, 1992. Janknecht, R., de Martynoff G., Lou, J., Hipskind, R.A., Nordheim, A., and Stunnenberg, H.G. Proc. Natl, Acad. Sci. U S.A. 88(20):8972-8976, 1991. Juliano, D., Wang, Y., Marcinkiewicz, C., Rosenthal, L.A., Stewart, G.J., and Niewiarowski, S. Exp. Cell Res. 225(1):132-142, 1996. Karczewski, J., Endris, R., and Connolly, T.M. J. Biol. Chem. 269(9):6702-6708, 1994. Kini, R.M. and Evans, H.J. Toxicon 30(3):265-293, 1992. Klaus, W., Broger, C., Gerber, P., and Senn, H. J. Mol. Biol. 232(3):897-906, 1993. Kloczewiak, M., Timmons, S., Bednarek, M.A., Sakon, M., and Hawiger, J. Biocheniistry 28(7):2915-2919, 1989. Kumar, CC., Nie, H., Rogers, C.P., Malkowski, M., Maxwell, E., Catino, J.J., and Armstrong, L. J. Pharrnacol. Exp. Ther. 283(2):843-853, 1997. Laemmli, U.K. Nature 227(259):680-685, 1970. Landt, O., Grunert, H.P., and Hahn, U. Gene 96(1):125-128, 1990. Laskowski, R. A., MacArthur M W, Moss D S & Thornton J M. J. Appl. Cryst, 26,283-291. 1993 Leavesley, D. I., Schwartz M. A. J. Cell Biol. 121:163-170. 1993. Li, H., Li, X., and Hu, M. I. Chuan,. Hsueh. Pao. 23(2):163-168, 1996. Ling, M. M., and Robinson, B.H. Anal. Biochem. 254(2):157-178, 1997. Lopez, J.A., Chung, D.W., Fujikawa, K., Hagen, F.S., Davie, E.W., and Roth, G.J. Proc. Natl. Acad. Sci. U.S.A. 85(7):2135-2139, 1988. Majerus, P. W. The Molecular Basis of Blood Disease pp689-721, W. B. Saunders Co., Philadelphia, PA., 1987 Marcinkiewicz, C., Vijay Kurnar, S., McLane, M.A., and Niewiarowski, S. Blood 90(4):1565-1575, 1997. Marini, F.,3d, Naeem, A., and Lapeyre, J.N. Nucleic. Acids. Res. 21(9):2277-2278, 1993. McLane, M.A., Vijay Kumar, S., Marcinkiewicz, C., Calvete, J.J., and Niewiarowski, S. FEBS Lett. 391(1-2):139-143, 1996. Meier, J., and Freyvogel, T.A. Toxicon 18(5-6):661-662, 1980. Michael, J., Bower, Fred E. Cohen and Roland L. Dunbrack, Jr J MB, v 267, n 5, Apr 1997, p 1268-1282 Modeller Release 4-A Program for Protein Structure Modeling ,A.?ali, Roberto Sanchez and Azat Badretdinov; the Rockefeller University. http:/guitar. rockefefeller. edu/ Molecular Simulations Inc. 9685 Scranton Road San Diego, CA 92121-3752 U.S.A. Web:http://www,msi.com. Musial, J., Niewiarowski, S., Rucinski, B., Stewart, G.J., Cook, J.J., Williams, J.A., Circulation 82(1):261-273, 1990. Niewiarowski, S., McLane, M.A., Kloczewiak, M., and Stewart, G.J. Semin. Hematol. 31(4):289-300, 1994. Oursler, M.J. and Spelsberg, T.C. Endocrinology 132(3):939-940, 1993. Ouyang, C.H., Ma, Y.H., Jih, H.C., and Teng, C.M. Biochim. Biophys. Acta 841(1):1-7, 1985. P,Clezardin. CMLS, Cell. Mol. Life Sci. 54; 541-548, 1998. Pfaff, M., McLane, M.A., Beviglia, L., Niewiarowski, S., and Timpl, R. Cell Adhes. Commun. 2(6):491-501, 1994. Pierschbacher, M.D., and Ruoslahti, E. Nature 309(5963):30-33, 1984. Plow, E.F., Pierschbacher, M.D., Ruoslahti, E., Marguerie, G.A., and Ginsberg, M.H. Proc. Natl. Acad. Sci. U.S.A. 82(23):8057-8061, 1985. Polverini, P. J., Am. J Pathol. 148:1023-1029.1996. Prodromou, C., and Pearl, L.H. Protein Eng. 5(8):827-829, 1992. Pugh, R.N., Theakston, R.D., and Reid, H.A. Ann. Trop. Med. Parasitol. 74(5):523-530, 1980. Roland Luthy, James U., Bowie, David Eisenberg., Nature, 356, 83-85, 1992. Ruggeri, Z.M., and Zimmerman, T.S. Blood 70(4):895-904, 1987. Ruoslahti, E. Integrins. J. Clin. Invest. 87(1):1-5, 1991. Ruoslahti, E. and Pierschbacher, M.D. Science 238(4826):491-497, 1987. Sali, A. and Blundell, T.L. J. Mol. Biol. 234(3):779-815, 1993. Sambrook, J., Fritsch, E. F., Maniatis, T. Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory Press. pp. 18.47-18.62, 1989 Samuel, I. Rapaport. “Introduction to Hematology” second Edition. Sarkar, G., and Sommer, S. More light on PCR contamination [letter]. Nature 347(6291):340-341, 1990. Sato, M., Sardana, M.K., Grasser, W.A., Garsky, V.M., Murray, J.M., and Gould, R.J. J. Cell Biol. 111(4):l713-1723, 1990. Sato, M., Garsky, V., Majeska, R.J., Einhorn, T.A., Murray, J., Tashjian, A.H., Jr., and Gould, R.J. J Bone Miner. Res. 9(9):1441-1449, 1994. Saudek, V., Atkinson, R.A., and Pelton, J.T. Biochemistiy 30(30):7369-7372, 1991. Saudek, V., Atkinson, R.A., Lepage, P., and Pelton, J.T. Eur. J. Biochem. 202(2):329-338, 1991. Saudek, V., Atkinson, R.A. and Pelton, J.T. Biochemistiy 30(30), 7369-7372 (1991) Savage, B., Marzec, U.M., Chao, B.H., Harker, L.A., Maraganore, J.M., and Ruggeri, Z.M. J. Biol. Chem. 265(20):11766-11772, 1990. Savage, B., and Ruggeri, Z.M. J. Biol. Chem. 266(17):11227-11233, 1991. Senn, H., and Klaus, W. J. Mol. Biol. 232(3):907-925, 1993. Staiano, N., Villani, G.R., Di Martino, E., Squillacioti, C., Vuotto, P., and Di Natale, P. Biochem. Mol. Biol. Int. 35(1):11-19, 1995. Staiano, N., Garbi, C., Squillacioti, C., Esposito, S., Di Martino, E., Belisario, M.A., Nitsch, L., and Di Natale, P. Eur. J. Cell Biol. 73(4):298-305, 1997. Tainer, R.A., Getzoff, E. D., s., H., Houghten, R.A., Olson, A. J., Lerner, R.A., and Hendrickson, W. A. Alexander. Nature 312, 127-134. Teng C-M, Huang T-F. Platelets 2:1-11, 1991. UHonig-B; Nicholls-A. Science, 268, 1144-1149, 1995. Vinals C, De Bolle X, Depiereux E, Feytmans E. Proteins 21:307-318. 1995. Warrell, D.A., Davidson, N.M., Greenwood, B.M., Ormerod, L.D., Pope, H.M., Watkins, B.J., and Prentice, C.R. O.J. Med. 46(181):33-62, 1977. Weiner, S. J., Kollman, P. A., Nguyen, D. T., Case, D. A., .J Comp. Chem. 7,230-52,1986 Werb Z., Tremble P. M. J. Cell Biol. 109:877-889, 1989. Weissman, J. S., & Kim, P. S. Nat. Struct. Biol 2,1123-1130. 1995. Wlodawer, A., Nacham, J., Gilliland, G. L., Galagher, W. & Woodward, C. J. Mol. Biol. 198, 469-480, 1987. Woody, R.W. in Peptides, polypeptides and proteins (Blout, E.R., Bovery, F.A., Goodman, M. & Lotan, N., eds) pp.338-350, Wiley, New York. Wright, P.S., Saudek, V., Owen, T.J., Harbeson, S.L., and Bitonti, A.J. Biochem. J. 293(Pt 1):263-267, 1993. Xi-Ping, Zhang., Tetsuji Kamata. J Biol. Chem.273:7345-7350, 1998. Yamada, T., Uyeda, A., Kidera, A., and Kikuchi, M. Biochemistry 33(39):11678-11683, 1994. Yamada, T., and Kidera, A. FEBS Lett. 387(1):11-15, 1996. Yamamoto, M., Fisher, J.E., Gentile, M., Seedor, J.G., Leu, C.T., Rodan, S.B., and Rodan, G.A. Endocrinology 139(3):1411-1419, 1998. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75019 | - |
dc.description.abstract | 我們利用PCR的技術,合成γ-echistatin的基因,並將此基因轉殖到pQE-30載體上,再將載體送入大腸桿菌(Escherichia coli)以表現所要探討的抗凝血蛇毒-γ-echistatin。轉殖後的菌落,以PCR篩選出含有γ-echistatin基因菌體,再利用核酸定序儀以確定送入的基因為正確。篩選出的大腸桿菌,以IPTG誘導菌體,大量表現出C端含有γ-echistatin勝?鍵的蛋白。我們先利用親和性管柱(Ni-NTA Column)將此蛋白純化出來,再經還原劑、透析處理之後,以蛋白?enterokinase將C端的γ-echistatin切下,在enterokinase緩衝液的條件下,切下的γ-echistatin將自行摺疊成具活性的結構。此摺疊完成的γ-echistatin以HPLC純化出來,經質譜儀(mass spectrometry)、圓偏光二色光譜(circula dichroism)、和抗凝血活性的測試,其結果皆與原先由毒蛇身上萃取出來的γ-echistatin具有相同的性質。 我們利用點突變(Site-irected mutagenesis)的技術得到六個突變株,其中一株表現出的蛋白質(R24K),是將第24個胺基酸由精胺酸(arginine)變成了由離胺酸(lysine),另外兩株表現的蛋白(NMA21.22.23 RPT and NMA21.22.23 RPS)是將第21,22和第23個胺基酸由天門冬素(asparagine)甲硫氨酸(methionine)氨基丙酸(alanine)分別變成了精胺酸(arginine)比胳氨酸(proline)丁氨酸(threonine)和精胺酸(arginine)比胳氨酸(proline)絲氨酸(serine)。 由於γ-echistatin是屬於含有精胺酸-甘胺酸-天門冬胺酸序列(RGD sequence)的抗凝血蛇毒(disintegrin),若將其中的精胺酸改成由離胺酸,經本實驗結果證實,抗凝血的活性會降低3倍以上。將第21,22和第23個胺基酸由原本的天門冬素(asparagin)甲硫氨酸(methionine)氨基丙酸(alanine)分別變成了精胺酸(arginine)比胳氨酸(proline)丁氨酸(threonine)和精胺酸(arginine )比胳氨酸(proline)絲氨酸(serine),實驗的結果指出活性大約降低8-12倍。因此我們推論,第21,22和23個胺基酸可能和RGD loop有協同的作用,使得γ-echistatin 對於血小板上的細胞膜蛋白integrin αIIbβ3有較弱的親和力,而抑制血小板的凝集。 根據過去的實驗,將γ-echistatin的C端,從第46個胺基酸之後切除或再將(Cys8-Cys37)這對雙硫鍵都改成氨基丙酸(alanine),活性都約降低1.7倍,並且我們從實驗結果及電腦模擬的γ-echistatin結構推測第7-32這對雙硫鍵(Cys7-cys32)或第8-37這對雙硫鍵(Cys8-Cys37)在γ-echistatin摺疊時只須一對存在即可。且從實驗結果可推測易最快形成的第2-11這對雙硫鍵會影響7-32這對雙硫鍵(Cys7-Cys32)或第8-37(Cys8-Cys37)這對雙硫鍵的形成。而且由實驗結果可推測20-39這對雙硫鍵(Cys20-Cys39)在蛋白質摺疊時可能扮演重要的角色。 | zh_TW |
dc.description.abstract | A gene encoding an RGD-containing platelet aggregation inhibitor, γ-echistatin, has been synthesized through PCR method using four overlapping oligonucleotides. The synthetic gene has Hind III sites at both ends for cloning into pQE-30 expression vector and an (Asp)4-Lys coding sequence recognized by enterokinase to cleave the fusion protein. The recombinant expression vector was transferred into M15 [pREP4] competent cells, the positive clones were identified by PCR and verified by DNA sequence analysis. After over-expression by inducing with IPTG, crude γ-echistatin fusion protein was purified through Ni-NTA column. The crude fusion protein was first denatured and reduced to prevent mis-linkage of disulfide bonds. Then γ-echistatin fusion protein was cleaved by enterokinase and refolded. The recombinant, mature γ-echistatin was purified to homogeneity by HPLC, and verified by CD spectrum and mass spectrometry. This recombinant γ-echistatin was also assayed for inhibiting platelet aggregation and found to be identical to that of native γ-echistatin. We also constructed the mutants of γ-echistatin R24N, C2A, C7A, C20A, NMA21.22.23 RPT and NMA21.22.23 RPS by site directed mutagenesis. The inhibitory potency of R24K mutant is only 3-fold less than that of the wild type. For the mutants, NMA21.22.23 RPT and NMA21.22.23 RPS, their inhibitory potency were decreased about 8-12 folds. Our previous research has pointed out that the disulfide bond (8-37) might not be necessary in platelet aggregation inhibition because the inhibitory potency of des(45-49)-γ-echistatin and des(45-49)-[Ala8,37]-γ-echistatin both decrease about 1.7- fold. In summary, according to our results and on the basis of the structural model of γ-echistatin we speculated there were needed three disulfide bonds (2-11, 7-32, 20-39) or (2-11, 8-37, 20-39) during the folding pathway of γ-echistatin. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:11:24Z (GMT). No. of bitstreams: 0 Previous issue date: 1999 | en |
dc.description.tableofcontents | 中文摘要…………1 Abstract…………3 List of Abbreviations…………4 Chapter 1: Introduction…………5 I. Motivations of the Dissertation…………6 II. Overview of the Integrins and Angiogenesis…………7 III. A Minireview of Echistatin…………10 The discovery of echistatin…………10 The synthetic and recombinant echistatin…………11 The structure of echistatin…………13 The overall structure of echistatin…………13 The important of RGD loop…………13 The importance of C-terminal domain of echistatin…………14 The disulfide bridges of echistatin…………15 IV. A Minireview of The Importance of Disuffide Bonds of Protein Folding Pathway…………16 Figures…………18 The interaction of echistatin 11 Chapter 2: The construction of γ-Echistatin…………23 I. PCR-based strategy for γ-echistatin gene synthesis…………24 Materials and Methods…………24 The megaprimer method…………24 Results and Discussion…………25 II. Cloning synthetic gene into pQE-30 vector…………27 Materials and Methods…………27 Ligation of the synthetic gene into pQE-30 vector…………27 Preparation of competent M15 [pREP4] cells…………28 Transformation…………28 Screening for positive clones…………29 Sequence analysis…………29 Results and Discussion…………29 Figures…………31 Chapter 3: The Expression of γ-Echistatin…………36 Materials and Methods…………37 Small-scale expression of γ-echistatin…………37 Growing large-scale expression culture…………37 Cell lysis and checking for cytoplasmic or periplasmic location…………37 Purification of cytoplasmic proteins by Ni-NTA column…………38 SDS-polyacrylamide gel electrophoresis…………38 Novex Tricine SDS Gel Electrophoresis…………39 The process of cleavage and refolding of γ-echistatin…………40 The modified process of cleavage and refolding of γ-echistatin…………40 Results and Discussion…………41 Expression of γ-echistatin…………41 Affinity purification of 6xHis-tagged proteins…………41 The process of cleavage and folding of recombinant γ-echistatin…………41 Figures…………43 Chapter 4: Site-Directed Mutagenesis of γ-Echistatin…………48 Materials and Methods…………64 Synthesis of oligonucletides…………49 Assembly of synthetic fragment by PCR…………49 Results and Discussion…………51 Site-directed mutagenesis…………51 Expression of R24K, C2A, C7A, C2OA, NMA21-23,,RPS,NMA21-23 RPT…………52 Purification of R24K, NMA21-23, RPS, NMA21-23, RPT…………52 LC-Mass of C2A, C7A and C20A…………52 Circular dichroism…………52 Figures…………53 Chapter 5: The Molecular Model of γ-Echistatin & its mutant…………64 Method…………65 Sequence alignment…………65 Initial model…………65 Model refinement…………66 Model evalution…………66 γ-Echistatin mutant modeling…………66 Result and Discusion………………67 Chapter 6: Biological activity of γ-Echistatin………………74 Materials and Methods………………75 Determining protein concentration………………75 Platelet aggregation assay………………76 Results………………76 Chapter 7: Discussion and Prospect………………77 Reference………………82 | |
dc.language.iso | zh-TW | |
dc.title | γ-Echistatin 突變株種的探討 | zh_TW |
dc.title | Study on γ-Echistatin mutants | en |
dc.date.schoolyear | 87-2 | |
dc.description.degree | 碩士 | |
dc.relation.page | 90 | |
dc.rights.note | 未授權 | |
dc.contributor.author-dept | 生命科學院 | zh_TW |
dc.contributor.author-dept | 生化科學研究所 | zh_TW |
顯示於系所單位: | 生化科學研究所 |
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