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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 宋延齡(Yen-Ling Song) | |
| dc.contributor.author | Meng-Yi Chen | en |
| dc.contributor.author | 陳夢怡 | zh_TW |
| dc.date.accessioned | 2021-06-13T17:01:04Z | - |
| dc.date.available | 2006-12-31 | |
| dc.date.copyright | 2005-02-04 | |
| dc.date.issued | 2005 | |
| dc.date.submitted | 2005-01-31 | |
| dc.identifier.citation | Reference List
1. Theopold U, Schmidt O, Soderhall K, Dushay MS: Coagulation in arthropods: defence, wound closure and healing. Trends Immunol 2004, 25: 289-294. 2. Tzou P, De Gregorio E, Lemaitre B: How Drosophila combats microbial infection: a model to study innate immunity and host-pathogen interactions. Current Opinion in Microbiology 2002, 5: 102-110. 3. Iwanaga S, Kawabata S: Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab. Front Biosci 1998, 3: D973-D984. 4. Tokunaga F, Yamada M, Miyata T, Ding YL, Hiranaga-Kawabata M, Muta T et al.: Limulus hemocyte transglutaminase. Its purification and characterization, and identification of the intracellular substrates. J Biol Chem 1993, 268: 252-261. 5. Yeh MS, Chen YL, Tsai IH: The hemolymph clottable proteins of tiger shrimp, Penaeus monodon, and related species. Comp Biochem Physiol B Biochem Mol Biol 1998, 121: 169-176. 6. Hall M, Wang R, van Antwerpen R, Sottrup-Jensen L, Soderhall K: The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood. Proc Natl Acad Sci U S A 1999, 96: 1965-1970. 7. Karlsson C, Korayem AM, Scherfer C, Loseva O, Dushay MS, Theopold U: Proteomic analysis of the drosophila larval hemolymph clot. J Biol Chem 2004. 8. Theopold U, Li D, Fabbri M, Scherfer C, Schmidt O: The coagulation of insect hemolymph. Cell Mol Life Sci 2002, 59: 363-372. 9. Wang R, Liang Z, Hal M, Soderhall K: A transglutaminase involved in the coagulation system of the freshwater crayfish, Pacifastacus leniusculus. Tissue localisation and cDNA cloning. Fish Shellfish Immunol 2001, 11: 623-637. 10. Folk JE, Finlayson JS: The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv Protein Chem 1977, 31: 1-133. 11. Folk JE: Transglutaminases. Annu Rev Biochem 1980, 49: 517-531. 12. Lorand L, Conrad SM: Transglutaminases. Mol Cell Biochem 1984, 58: 9-35. 13. Greenberg CS, Birckbichler PJ, Rice RH: Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991, 5: 3071-3077. 14. Song YL, Yu CI, Lien TW, Huang CC, Lin MN: Haemolymph parameters of Pacific white shrimp (Litopenaeus vannamei) infected with Taura syndrome virus. Fish Shellfish Immunol 2003, 14: 317-331. 15. Kuo-Kau Lee, Yi-Ling Chen, Ping-Chung Liu: Hemostasis of Tiger Prawn Penaeus monodon Affected by Vibrio harveyi, Extracellular Products and a Toxic Cysteine Protease. Blood Cells, Molecules, and Diseases 1999, 15: 180-192. 16. Tait J: Types of crustacean blood coagulation. J Mar Biol Assoc U K 1911, 9: 191-198. 17. Sidne A.Omori, Gary G.Martin, Jo Ellen Hose: Morphology of hemocyte lysis and clotting in the ridge back prawn, Sicyonia ingentis. Cell Tissue Res 1989, 255: 117-123. 18. Grenard P, Bates MK, Aeschlimann D: Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z. J Biol Chem 2001, 276: 33066-33078. 19. Esposito C, Pucci P, Amoresano A, Marino G, Cozzolino A, Porta R: Transglutaminase from rat coagulating gland secretion. Post-translational modifications and activation by phosphatidic acids. J Biol Chem 1996, 271: 27416-27423. 20. Kim SY, Chung SI, Steinert PM: Highly active soluble processed forms of the transglutaminase 1 enzyme in epidermal keratinocytes. J Biol Chem 1995, 270: 18026-18035. 21. Steinert PM, Kim SY, Chung SI, Marekov LN: The transglutaminase 1 enzyme is variably acylated by myristate and palmitate during differentiation in epidermal keratinocytes. J Biol Chem 1996, 271: 26242-26250. 22. Kanaide H, Shainoff JR: Cross-linking of fibrinogen and fibrin by fibrin-stablizing factor (factor XIIIa). J Lab Clin Med 1975, 85: 574-597. 23. Nielsen VG, Gurley WQ, Jr., Burch TM: The impact of factor XIII on coagulation kinetics and clot strength determined by thrombelastography. Anesth Analg 2004, 99: 120-123. 24. Wettstein P, Haeberli A, Stutz M, Rohner M, Corbetta C, Gabi K et al.: Decreased factor XIII availability for thrombin and early loss of clot firmness in patients with unexplained intraoperative bleeding. Anesth Analg 2004, 99: 1564-1569. 25. Koh D, Inohaya K, Imai Y, Kudo A: The novel medaka transglutaminase gene is expressed in developing yolk veins. Gene Expr Patterns 2004, 4: 263-266. 26. Candi E, Melino G, Mei G, Tarcsa E, Chung SI, Marekov LN et al.: Biochemical, structural, and transglutaminase substrate properties of human loricrin, the major epidermal cornified cell envelope protein. J Biol Chem 1995, 270: 26382-26390. 27. Tarcsa E, Marekov LN, Andreoli J, Idler WW, Candi E, Chung SI et al.: The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases. J Biol Chem 1997, 272: 27893-27901. 28. Achyuthan KE, Greenberg CS: Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J Biol Chem 1987, 262: 1901-1906. 29. Melino G, Piacentini M: 'Tissue' transglutaminase in cell death: a downstream or a multifunctional upstream effector? FEBS Lett 1998, 430: 59-63. 30. Ho KC, Quarmby VE, French FS, Wilson EM: Molecular cloning of rat prostate transglutaminase complementary DNA. The major androgen-regulated protein DP1 of rat dorsal prostate and coagulating gland. J Biol Chem 1992, 267: 12660-12667. 31. Mandal D, Moitra PK, Basu J: Mapping of a spectrin-binding domain of human erythrocyte membrane protein 4.2. Biochem J 2002, 364: 841-847. 32. Rybicki AC, Schwartz RS, Qiu JJ, Gilman JG: Molecular cloning of mouse erythrocyte protein 4.2: a membrane protein with strong homology with the transglutaminase supergene family. Mamm Genome 1994, 5: 438-445. 33. Inoue T, Kanzaki A, Yawata A, Tsuji A, Ata K, Okamoto N et al.: Electron microscopic and physicobiochemical studies on disorganization of the cytoskeletal network and integral protein (band 3) in red cells of band 4.2 deficiency with a mutation (codon 142: GCT-->ACT). Int J Hematol 1994, 59: 157-175. 34. Risinger MA, Dotimas EM, Cohen CM: Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem 1992, 267: 5680-5685. 35. Najfeld V, Ballard SG, Menninger J, Ward DC, Bouhassira EE, Schwartz RS et al.: The gene for human erythrocyte protein 4.2 maps to chromosome 15q15. Am J Hum Genet 1992, 50: 71-75. 36. Ambron RT, Kremzner LT: Post-translational modification of neuronal proteins: evidence for transglutaminase activity in R2, the giant cholinergic neuron of Aplysia. Proc Natl Acad Sci U S A 1982, 79: 3442-3446. 37. Singer MA, Hortsch M, Goodman CS, Bentley D: Annulin, a protein expressed at limb segment boundaries in the grasshopper embryo, is homologous to protein cross-linking transglutaminases. Dev Biol 1992, 154: 143-159. 38. Sugino H, Terakawa Y, Yamasaki A, Nakamura K, Higuchi Y, Matsubara J et al.: Molecular characterization of a novel nuclear transglutaminase that is expressed during starfish embryogenesis. Eur J Biochem 2002, 269: 1957-1967. 39. Battaglia DE, Shapiro BM: Hierarchies of protein cross-linking in the extracellular matrix: involvement of an egg surface transglutaminase in early stages of fertilization envelope assembly. J Cell Biol 1988, 107: 2447-2454. 40. Mozingo NM, Chandler DE: Evidence for the existence of two assembly domains within the sea urchin fertilization envelope. Dev Biol 1991, 146: 148-157. 41. Mehta K, Rao UR, Vickery AC, Birckbichler PJ: Significance of transglutaminase-catalyzed reactions in growth and development of filarial parasite, Brugia malayi. Biochem Biophys Res Commun 1990, 173: 1051-1057. 42. Fesus L: Biochemical events in naturally occurring forms of cell death. FEBS Lett 1993, 328: 1-5. 43. Iwanaga S, Kawabata S, Muta T: New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem (Tokyo) 1998, 123: 1-15. 44. Muta T, Iwanaga S: The role of hemolymph coagulation in innate immunity. Curr Opin Immunol 1996, 8: 41-47. 45. Muta T, Iwanaga S: Clotting and immune defense in Limulidae. Prog Mol Subcell Biol 1996, 15: 154-189. 46. Iwanaga S: The limulus clotting reaction. Curr Opin Immunol 1993, 5: 74-82. 47. Iwanaga S, Miyata T, Tokunaga F, Muta T: Molecular mechanism of hemolymph clotting system in Limulus. Thromb Res 1992, 68: 1-32. 48. Davids BJ, Mehta K, Fesus L, McCaffery JM, Gillin FD: Dependence of Giardia lamblia encystation on novel transglutaminase activity. Mol Biochem Parasitol 2004, 136: 173-180. 49. Tokunaga F, Muta T, Iwanaga S, Ichinose A, Davie EW, Kuma K et al.: Limulus hemocyte transglutaminase. cDNA cloning, amino acid sequence, and tissue localization. J Biol Chem 1993, 268: 262-268. 50. Osaki T, Okino N, Tokunaga F, Iwanaga S, Kawabata S: Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin. J Biol Chem 2002, 277: 40084-40090. 51. Adams MD, Celniker SE, Holt RA, Evans CA, Gocayne JD, Amanatides PG et al.: The genome sequence of Drosophila melanogaster. Science 2000, 287: 2185-2195. 52. Holt RA, Subramanian GM, Halpern A, Sutton GG, Charlab R, Nusskern DR et al.: The genome sequence of the malaria mosquito Anopheles gambiae. Science 2002, 298: 129-149. 53. Huang CC, Sritunyalucksana K, Soderhall K, Song YL: Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase. Dev Comp Immunol 2004, 28: 279-294. 54. Rojtinnakorn J, Hirono I, Itami T, Takahashi Y, Aoki T: Gene expression in haemocytes of kuruma prawn, Penaeus japonicus, in response to infection with WSSV by EST approach. Fish Shellfish Immunol 2002, 13: 69-83. 55. Rao RU, Mehta K: Transglutaminases, thioredoxins and protein disulphide isomerase: diverse enzymes with a common goal of cross-linking proteins in lower organisms. Indian J Exp Biol 2004, 42: 235-243. 56. Eschenlauer SC, Page AP: The Caenorhabditis elegans ERp60 homolog protein disulfide isomerase-3 has disulfide isomerase and transglutaminase-like cross-linking activity and is involved in the maintenance of body morphology. J Biol Chem 2003, 278: 4227-4237. 57. Wada F, Nakamura A, Masutani T, Ikura K, Maki M, Hitomi K: Identification of mammalian-type transglutaminase in Physarum polycephalum. Evidence from the cDNA sequence and involvement of GTP in the regulation of transamidating activity. Eur J Biochem 2002, 269: 3451-3460. 58. Teshigawara K, Kannagi R, Noro N, Masuda T: Possible involvement of transglutaminase in endocytosis and antigen presentation. Microbiol Immunol 1985, 29: 737-750. 59. Wirth JJ, Kierszenbaum F: Stimulatory effects of retinoic acid on macrophage interaction with blood forms of Trypanosoma cruzi: involvement of transglutaminase activity. J Immunol 1986, 137: 3326-3331. 60. Messick JB, Rikihisa Y: Characterization of Ehrlichia risticii binding, internalization, and proliferation in host cells by flow cytometry. Infect Immun 1993, 61: 3803-3810. 61. Szondy Z, Sarang Z, Molnar P, Nemeth T, Piacentini M, Mastroberardino PG et al.: Transglutaminase 2-/- mice reveal a phagocytosis-associated crosstalk between macrophages and apoptotic cells. Proc Natl Acad Sci U S A 2003, 100: 7812-7817. 62. Sarvary A, Szucs S, Balogh I, Becsky A, Bardos H, Kavai M et al.: Possible role of factor XIII subunit A in Fcgamma and complement receptor-mediated phagocytosis. Cell Immunol 2004, 228: 81-90. 63. Budzynski AZ: Fibrinogen and fibrin: biochemistry and pathophysiology. Crit Rev Oncol Hematol 1986, 6: 97-146. 64. Monsonego A, Mizrahi T, Eitan S, Moalem G, Bardos H, Adany R et al.: Factor XIIIa as a nerve-associated transglutaminase. FASEB J 1998, 12: 1163-1171. 65. D'Argenio G, Grossman A, Cosenza V, Valle ND, Mazzacca G, Bishop PD: Recombinant factor XIII improves established experimental colitis in rats. Dig Dis Sci 2000, 45: 987-997. 66. Phillips MA, Stewart BE, Qin Q, Chakravarty R, Floyd EE, Jetten AM et al.: Primary structure of keratinocyte transglutaminase. Proc Natl Acad Sci U S A 1990, 87: 9333-9337. 67. Liu S, Cerione RA, Clardy J: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci U S A 2002, 99: 2743-2747. 68. Ahvazi B, Boeshans KM, Idler W, Baxa U, Steinert PM: Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme. J Biol Chem 2003, 278: 23834-23841. 69. Yee VC, Pedersen LC, Le T, I, Bishop PD, Stenkamp RE, Teller DC: Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc Natl Acad Sci U S A 1994, 91: 7296-7300. 70. Noguchi K, Ishikawa K, Yokoyama K, Ohtsuka T, Nio N, Suzuki E: Crystal structure of red sea bream transglutaminase. J Biol Chem 2001, 276: 12055-12059. 71. Falquet L, Pagni M, Bucher P, Hulo N, Sigrist CJ, Hofmann K et al.: The PROSITE database, its status in 2002. Nucleic Acids Res 2002, 30: 235-238. 72. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W et al.: Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25: 3389-3402. 73. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG: The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 25: 4876-4882. 74. Kumar S, Tamura K, Jakobsen IB, Nei M: MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 2001, 17: 1244-1245. 75. Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72: 248-254. 76. Sung HH, Chang HJ, Her CH, Chang JC, Song YL: Phenoloxidase activity of hemocytes derived from Penaeus monodon and Macrobrachium rosenbergii. J Invertebr Pathol 1998, 71: 26-33. 77. Eberhard Spiess, Hans-Peter Zimmermann, Heinrich Lunsdorf: Negative Staining of Protein Molecules and FIlaments. In Electron Microscopy in Molecular Biology. Edited by J Sommerville, U Scheer. Oxford, Washington DC: IRL Press; 1987:147-166. 78. Nishimura T, Horino K, Nishiura H, Shibuya Y, Hiraoka T, Tanase S et al.: Apoptotic cells of an epithelial cell line, AsPC-1, release monocyte chemotactic S19 ribosomal protein dimer. J Biochem (Tokyo) 2001, 129: 445-454. 79. Song YL, Yu CI, Lien TW, Huang CC, Lin MN: Haemolymph parameters of Pacific white shrimp (Litopenaeus vannamei) infected with Taura syndrome virus. Fish Shellfish Immunol 2003, 14: 317-331. 80. Eckert KA, Kunkel TA: High fidelity DNA synthesis by the Thermus aquaticus DNA polymerase. Nucleic Acids Res 1990, 18: 3739-3744. 81. Adany R, Bardos H: Factor XIII subunit A as an intracellular transglutaminase. Cell Mol Life Sci 2003, 60: 1049-1060. 82. Kim IG, Lee SC, Lee JH, Yang JM, Chung SI, Steinert PM: Structure and organization of the human transglutaminase 3 gene: evolutionary relationship to the transglutaminase family. J Invest Dermatol 1994, 103: 137-142. 83. Spring J: Vertebrate evolution by interspecific hybridisation--are we polyploid? FEBS Lett 1997, 400: 2-8. 84. Gibson TJ, Spring J: Evidence in favour of ancient octaploidy in the vertebrate genome. Biochem Soc Trans 2000, 28: 259-264. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/39082 | - |
| dc.description.abstract | 凝血反應的快捷，可使生物有效防止受傷或感染後體液流失及微生物侵入體腔，此機制對只具有先天性免疫反應的無脊椎動物尤為重要。凝血系統的組成與活化在不同種的無脊椎動物中差異頗大，然而轉麩醯胺酵素 (transglutaminase, TG) (EC 2.3.2.13)卻是其中唯一保守的成員。TG催化形成分子間或分子內的ε-(γ-glutamyl) lysine 鍵結，使蛋白質聚合，其已知的生理功能則包括凝血和蛋白質轉譯後的修飾。我們由草蝦血球cDNA中選殖出一段TG序列，命名為草蝦第二型轉麩醯胺酵素（Shrimp Transglutaminase II, STG II），譯碼區含2,274個核苷酸，轉譯出的蛋白質含757個胺基酸，預測分子量約85,000 Da，等電點5.48。RT-PCR結果顯示STG II主要在血球而非肝胰臟表現，組織表現型式與STG I不相同。Neighbor Joining分析指出草蝦STG II和STG I之間的遺傳距離遠大於草蝦STG II和斑節蝦TG的距離，暗示草蝦的兩個TG可能位於染色體上不同的基因座。我們利用昆蟲-桿狀病毒表現系統得到重組STG II。穿透式電顯觀察發現重組的STG II能夠聚合凝血蛋白(clottable protein, CP, 萃取自草蝦血漿)形成一長鏈，型態相似於草蝦血球萃取液作用於血漿的凝血產物。本研究顯示草蝦的第二型轉麩醯胺酵素屬於血球型TG，參與凝血反應。 | zh_TW |
| dc.description.abstract | Coagulation (clot formation) can form a physical barrier to prevent the loss of body fluid and dissemination of microbes into the hemocoel after injury or infection. Its quickness and efficiency is essential for survival of invertebrates that relay solely on the innate immunity. Though the components and activation of coagulation system is diversified in the invertebrates, transglutaminase (TG) (EC 2.3.2.13) is the only conserved member throughout the known species. TG catalyzes intermolecular or intramolecular ε-(γ-glutamyl) lysine bond formation, resulting in protein polymerization. Physiologically, they are known for the roles in blood coagulation and post-translational protein modification. In the present study, we cloned a TG from shrimp (Penaeus monodon) hemocyte cDNA. It was assigned shrimp transglutaminase II (STG II). The TG cDNA consists of a coding region of 2,274 bp. The deduced protein has 757 amino acid residues, a calculated molecular mass of 85,000 Da and an isoelectric point of 5.48. RT-PCR results showed a high level of STG II expression in hemocytes, but not in hepatopancreas, differently from STG I. Neighbor Joining analysis indicates the genetic distance between STG II and STG I is much larger than that between STG II and TG of kuruma shrimp (Marsupenaeus japonicus). These evidences suggest at least two types of shrimp TG encoded from different chromosomal loci. The recombinant STG II was expressed using insect-baculovirus expression system. It showed polymerization activity on clottable proteins extracted from shrimp plasma. Under TEM observation, the polymerized chain resembles structurally the reacting products from shrimp hemocyte lysate supernatants on their plasma. Conclusively, STG II is characterized to be a hemocytic TG and involved in coagulation. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T17:01:04Z (GMT). No. of bitstreams: 1 ntu-94-R92b41014-1.pdf: 841309 bytes, checksum: 99d5ade6909e031c787c90973b0239fc (MD5) Previous issue date: 2005 | en |
| dc.description.tableofcontents | 摘要 3
略語及Accession Number清單 5 1. 背景與研究目的 6 甲殼類凝血可分三型 6 蝦類的凝血 7 哺乳動物中已知有九種TG 8 無脊椎動物TG的研究現況 8 TG是一個重要的防禦基因 9 TG基因的演化 10 TG的蛋白質結構與功能 11 研究目的 11 2. 材料與方法 12 2.1 血球cDNA的製備和STG II譯碼區的選殖 12 2.2 序列分析與比較 12 2.3 以RT-PCR偵測STG II的組織分布 12 2.4 重組STG II的表現與純化 12 2.5 草蝦凝血蛋白的純化，及草蝦血球萃取物的製備 13 2.6 DCA標定法（Dansylcadaverine Incorporation）測定TG活性 14 2.7 以穿透式電子顯微鏡觀察凝血活性 14 3. 結果 15 3.1 STG II序列分析 15 3.2 STG II與其他物種之TG的類緣關係 19 3.3 STG II的組織分布 22 3.4 STG II的表現純化及凝血蛋白的純化 22 3.5 STG II的酵素活性 22 3.6 STG II與凝血 25 4. 討論 27 TG催化聚合凝血產物的特性 27 同功酶的來源?Allelic variation? Loci variation? Individual variation? 29 鈣活化部位比對的不一致 30 由催化核心功能區塊辨認出的專一性片段，有何結構、功能、演化上的意義嗎？ 31 無脊椎動物TG可能會有幾種？STG II又是那一種TG呢? 32 不同物種凝血系統的比較 35 5. 結論與展望 35 | |
| dc.language.iso | zh-TW | |
| dc.subject | coagulation | zh_TW |
| dc.subject | Invertebrate | zh_TW |
| dc.subject | transglutaminase | zh_TW |
| dc.subject | clottable protein | zh_TW |
| dc.subject | clotting | zh_TW |
| dc.subject | 無脊椎動物 | en |
| dc.subject | 草蝦凝血蛋白 | en |
| dc.subject | 凝血 | en |
| dc.subject | 轉麩醯胺酵素 | en |
| dc.title | 無脊椎動物有一種以上的TG?草蝦第二型轉麩醯胺酵素參與凝血反應 | zh_TW |
| dc.title | More Than One Type of Transglutaminase in Invertebrates? A Second Type of Transglutaminase is Involved in Shrimp Coagulation | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 93-1 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 蔡國珍,胡光宇,陳建源,蔡郁惠 | |
| dc.subject.keyword | Invertebrate,transglutaminase,clottable protein,clotting,coagulation, | zh_TW |
| dc.subject.keyword | 無脊椎動物,轉麩醯胺酵素,凝血,草蝦凝血蛋白, | en |
| dc.relation.page | 44 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2005-02-02 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 動物學研究研究所 | zh_TW |
| 顯示於系所單位： | 動物學研究所 | |
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