(3.231.29.122) 您好!臺灣時間:2021/02/25 16:51
字體大小: 字級放大   字級縮小   預設字形  
回查詢結果

詳目顯示:::

我願授權國圖
: 
twitterline
研究生:曾俊銘
研究生(外文):Chun-Ming Tseng
論文名稱:利用人造油體系統製備蜂王漿抗菌胜&;#32957;royalisin之抗體與王漿抗菌胜&;#32957;之二級結構功能探討
論文名稱(外文):Preparation of a polyclonal antibody against royalisin, an antimicrobial peptide from royal jelly of Apis mellifera via an artificial oil body system and characterization of its functional secondary structure
指導教授:曾志正曾志正引用關係
指導教授(外文):Jason T. C. Tzen
學位類別:碩士
校院名稱:國立中興大學
系所名稱:生物科技學研究所
學門:生命科學學門
學類:生物科技學類
論文種類:學術論文
論文出版年:2010
畢業學年度:98
語文別:中文
論文頁數:84
中文關鍵詞:王漿抗菌胜&;#32957王漿抗菌胜&;#32957王漿抗菌胜&;#32957王漿抗菌胜&;#32957
外文關鍵詞:honeybeeApis melliferahypopharyngeal glandroyalisinartificial oil body antigen display system
相關次數:
  • 被引用被引用:1
  • 點閱點閱:147
  • 評分評分:系統版面圖檔系統版面圖檔系統版面圖檔系統版面圖檔系統版面圖檔
  • 下載下載:0
  • 收藏至我的研究室書目清單書目收藏:0
王漿抗菌胜&;#32957;(Royalisin)為蜜蜂工蜂下咽頭腺分泌的抗菌胜&;#32957;,其由51胺基酸所組成,大小為5.5 kDa,其中有6個半胱胺酸(cysteine) 組成三個分子內的雙硫鍵,使其結構及活性相當穩定。由於royalisin為小片段胜&;#32957;,為了提高動物對此小胜&;#32957;所產生的免疫反應,因此,本研究利用人造油體抗原呈現系統來製備royalisin的抗體。我們利用基因工程分別將royalisin架構到油體膜蛋白質oleosin中間疏水區域的N端及C端,形成royalisin-OleC-royalisin之融合蛋白質,並藉由大腸桿菌表現系統大量表現及純化。因為佐劑含有礦物油,而融合蛋白質與油混合均質化後會形成乳糜球,疏水性油體膜蛋白質中央區則會插入到油質中,並將N端及C端的royalisin展現在油體的表面,形成一個人造油體抗原呈現系統,以此系統製備抗體將有助於增加免疫系統辨識到小片段胜&;#32957;的能力而產生抗體。結果發現,製備出的抗體可專一的辨認到重組的王漿抗菌胜&;#32957;及天然蜂王漿中的王漿抗菌胜&;#32957;,王漿抗菌胜&;#32957;的專一性抗體將有助於王漿抗菌胜&;#32957;的研究及特性分析。本研究亦利用人造油體系統純化重組王漿抗菌胜&;#32957;,經由DTT處理,探討二級結構對於王漿抗菌胜&;#32957;抗菌活性的影響,結果發現雙硫鍵的保留與其抗菌活性有相當的關係。

Royalisin is the small peptides secreted by hypopharyngeal gland of Apis mellifera. It contains 51 amino acid residues with 6 cysteine residues forming three intramolecular disulfide linkages, perhaps resulting in a compact globular structure exhibiting high stability at low pH and high temperature. Since royalisin was small peptide, it is not easy to prepare its corresponding antibody. In this study, we want to prepare a specific antibody against to small peptide royalisin via artificial oil body. Royalisin was constructed to the N- and C-terminal of oleosin central hydrophobic domain as the oleosin fusion protein, royalisin-oleosin central domain-royalisin (Roy-OleC-Roy). Roy-OleC-Roy fusion protein was expressed and purified in E. coli AD494 (DE3). The purified fusion protein was mixed with Freund’s adjuvant to form emulsion and used for the production of antibody in chicken. In this system, oleosin is used as the carrier which possesses a lipophilic segment embedded in the hydrophobic oil core and the royalisin which linking to the two arms protruding on the surface of the oil bodies. In results, we have successfully to prepare the antibodies to against small antimicrobial peptide royalisin by this antigen display system. This antibody can be useful for study and characteristic analysis of royalisin. In this study, we also purified an antimicrobial peptide-royalisin via an artificial oil body system, and treat with the reducing agent dithiothreitol(DTT). As results show the disulfide bonds are very important for antimicrobial activity of royalisin.

中文摘要 i
Abstract ii
目次 iii
壹、緒論 1
1.1 蜂王漿 1
1.2 王漿抗菌胜肽(Royalisin) 2
1.3 油體簡介 3
1.4 油體膜蛋白(oleosin)介紹及其相關應用 4
1.5 抗體製備系統 12
1.6 研究動機 15
貳、材料與方法 17
2.1 油體膜蛋白載體之構築 17
2.2 構築表現載體-pJ01-roy-OleC-roy 18
2.2.1 利用聚合酶連鎖反應(PCR)選殖royalisin序列 18
2.2.2 瓊脂凝膠電泳分析與回收 18
2.2.3 DNA接合作用 19
2.2.4 轉型作用與藍白篩選 19
2.2.5 重組質體之回收 20
2.2.6 構築含有融合蛋白質roy-OleC-roy之表現載體 21
2.3 融合蛋白質Roy-OleC-Roy的表達及純化 21
2.3.1 微生物之大量表現 21
2.3.2 融合蛋白質之純化 23
2.4 人造油體穩定性測試 24
2.4.1 磷脂質與芝麻油的製備 24
2.4.2 人造油體之重組 24
2.4.3 油體的穩定性測試 25
2.5 抗體的製備及回收 25
2.5.1 蛋白質濃度測定 25
2.5.2 多株抗體(Polyclonal antibody)之製備 26
2.5.3 多株抗體之純化與回收 26
2.6 西方墨點法(western blot) 27
2.6.1 Tricine-SDS-PAGE 27
2.6.2 西方墨點法測試 28
2.7 重組王漿抗菌胜肽的純化與抗菌分析 29
2.7.1 融合蛋白質oleosin-inteinS-royalisin表達 30
2.7.2 融合蛋白質(royalisin-inteinS-oleosin)之純化 30
2.7.3 重組王漿抗菌胜肽之純化 31
2.7.4 最低抑菌濃度測試(Minimal inhiboitory concentration, MIC) 32
2.7.5 最低殺菌濃度(Minimal Bactericidal Concentration Assay,MBC) 33
2.7.6 重組王漿抗菌胜肽-Royalisin之蛋白質殺菌動力學分析(Time kill determination) 34
2.7.7 胰蛋白質水解酶對重組王漿抗菌胜肽之影響 35
參、實驗結果 36
3.1 royalisin抗體製備純化與分析 36
3.1.1 攜帶子蛋白質載體之構築 36
3.1.2 構築融合蛋白質(roy-OleC-roy)的表現載體 36
3.1.3 大量表現及純化融合蛋白質(roy-OleC-roy) 37
3.1.4 人造油體的穩定性測試 38
3.2 重組王漿抗菌胜肽royalisin二級結構對抗菌活性的影響 41
3.2.1 重組王漿抗菌胜肽的抑菌及殺菌所需最低濃度測試 41
3.2.2 蛋白質殺菌動力學分析(Time kill kinetic assay) 46
3.2.3 經Trypsin處理後重組王漿抗菌胜肽的最低抑菌濃度測試 48
肆、討論 49
4.1 以人造油體系統作為抗原呈現系統來製備小胜肽的抗體 49
4.2 以人造油體純化系統統純化出具有活性的雙硫鍵抗菌胜肽 50
4.3 重組王漿抗菌胜肽具有開發成為新型抗菌藥物的潛力 51
4.4提高人造油體蛋白質表達及純化系統的回收效率 53
4.5 探討重組王漿抗菌胜肽其雙硫鍵與抗菌活性之分析 54
參考文獻 56
圖表 66
表一、本研究所使用的引子 67
表二、本研究所使用測試抗菌活性之菌種 68
表三、重組王漿抗菌胜肽對11種細菌之抗菌作用 69
圖一、攜帶子蛋白質載體pET-29-OleC之構築 70
圖二、表現載體pJ01-roy-OleC-roy構築之流程圖 71
圖三、SDS-PAGE電泳分析融合蛋白質(roy-OleC-roy)在大腸桿菌AD494之表現 72
圖四、溫度對人造油體之穩定性分析 74
圖五、royalisin抗體對天然蜂王漿專一性之分析 75
圖六、SDS-PAGE電泳分析融合蛋白質(roy-inteinS-Ole)在大腸桿菌AD494之表現 76
圖七、西方墨點法分析由人造油體蛋白質純化系統之重組王漿抗菌胜肽 77
圖八、革蘭氏陽性菌存活率試驗 78
圖九、革蘭氏陰性菌存活率試驗 79
附錄 80
附錄一、油體膜蛋白質oleosin之二級結構圖 81
附錄二、人造油體蛋白質表達及純化系統的構築示意圖 82
附錄三、人造油體抗原展現系統的示意圖 83
附錄四、royalisin抗體之架構示意圖 84


[1]Haydak, M.H. ( 1970) Honey bee nutrition. Ann. Rev. Entomol. 15, 143-156
[2]Bilikova, K., Hanes, J., Nordhoff, E., Saenger, W., Klaudiny, J., Simuth, J. (2002) Apisimin, a new serine–valine-rich peptide from honeybee(Apis mellifera L) Royal Jelly: Purification and Molecular Characterization. FEBS Lett. 528, 125-129
[3]Blum, M. S., Novak, A. F., Taber, S. (1959) 10-Hydroxy-2Δ-decenoic acid, an antibiotic found in royal jelly. Science, 130, 452- 453
[4]Fujiwara, S., Imai, J., Fujiwara, M., Yaeshima, T., Kawashima, T. ., Kobayashi, K. (1990) A potent antibacteria protein in royal jelly:Purification and determination of the primary sturacture of royalisin. J, boil. chem. 265, 11333-11337
[5]Bilikova, K., Gusui, W., Simuth, J. (2001) Isolation of a peptide fraction from honeybee royal jelly as a potential antifoulbrood factor. Apidologie. 32, 275-283
[6]Bulet, P., Hetru, C., Dimarcq, J. L., Hoffmann, D. (1999) Antimicrobial peptides in insects; structure and function. Dev. Comp. Immunol. 23, 329-344
[7]Casteels, P., Ampe, C., Jacobs, F., Vaek, M., Tempst, P. (1989) Apidaecins: antibacterial peptides from honeybee. EMBO J. 8, 2387-2391
[8]Casteels, P., Ampe, C., Riviere, L., Damme, J.V., Elicone, C., Fleming, M., Jacobs, F., Tempst, P. (1990) Isolation and characterization of abaecin, a major antibacterial peptide in the honeybee (Apis mellifera). Eur. J. Biochem. 187, 381-386
[9]Casteels, P., Ampe, C., Jacobs, F., Tempst, P. (1993) Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the Apis mellifera. J. Biol. Chem. 268, 7744-7054
[10]Casteels-Jasson, K., Zhang, W., Capaci, T., Casteels, P., Tempst, P. (1994) Acute transcriptional response of the honeybee peptide-antibiotics gene repertorire and required post-translational conversion of the precursor structures. J. Biol. Chem. 269, 28569-28575
[11]Bachanova, K., Klaudiny, J., Kopernicky, J., Simuth, J. (2002) Identification of honeybee peptide active against Paenibacillus larvae larvae through bacterial growth-inhibition assay on polyacrylamide gel. Apidologie 33, 259-269
[12]Klaudiny, J., Albert, S., Bachanova, K., Kopernicky, J., Simuth, J. (2005) Two structurally different defensin genes, one of them encoding a novel defensin isoform, are expressed in honeybee Apis mellifera. Insect Biochemistry and Molecular Biology 35, 11-22
[13]Hanzawa, H., Shimada, I., Kuzuhara, T., Komano, H., Kohda, D., Inagaki, F., Natori,S., Arata, Y. (1990) 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin. FEBS Lett. 269, 413–420
[14]Bonmatin, J.M., Bonnat, J.L., Gallet, X., Vovelle, F., Ptak, M., Reichart, J.M., Hoffmann, J. A., Keppi, E., Legrain, M., Achstetter, T. (1992) Two-dimensional 1H NMR study of recombinant insect defensin A in water: resonance assignments, secondary structure and global folding. J. Biomol. 2, 235–256
[15]Cornet, B., Bonmatin, J.M., Hetru, C., Hoffmann, J.A., Ptak, M., Vovelle, F.,(1995) Refined three-dimensional solution structure of insect defensin A. Structure 3, 435–448
[16]Cociancich, S., Ghazi, A., Hetru, C., Hoffmann, J.A., Letellier, L. (1993) Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 268, 19239-19245
[17]Tzen, J. T. C., Peng C.C., Cheng, D.J., Chen, E.C., Chiu J.M. (1997) A new method forseed oil body purification and examination of oil body integrity following germination. J. Biochem. 121, 762-768
[18]Tzen, J. T. C., Cao, Y. Z., Laurent, P., Ratnayake, C. and Huang, A. H.C. (1993) Lipids, proteins, and structure of seed oil bodies from diverse species. Plant Physiol. 101, 267-276
[19]Peng, C. C., Tzen, J. T. C. (1998) Analysis of the three essential constituents of oil bodies in developing sesame seeds. Plant Cell Physiology 39, 35-42
[20]Slack, C. R., Bertaud, W. S., Shaw, B. P., Holland, R., Browse, J. andWright, H. (1980) Some studies on the composition and surface properties of oil bodies from the seed cotyledons of safflower andlinseed. J Biol Chem. 190, 551-561
[21]Tzen, J. T. C., Líe GC., Huang AHC (1992) Characterization of the charged components and their topology on the surface of plant seed oil bodies. J Biol Chem. 267, 15626-15634
[22]Tzen, J. T. C., Chuang, R. L. C., Chen, J. C. F., Wu, L. S. H. (1998) Coexistence of both oleosin isoforms on the surface of seed oil bodies and their individual stabilization to the organelles. J. Biochem. 123, 319-324
[23]Qu, R., Wang, S. M., Lin, Y. H., Vance, V. B., Huang, A. H. C. (1986) Characteristics and biosynthesis of membrane proteins of lipid bodies in the scutella of maize (Zea mays L.). Biochem. J. 234, 57-65
[24]Murphy, D. J., Au, D. M. Y. (1989) A new class of highly abundant apolipoproteins involved in lipid storage in oilseeds. Biochem. Soc.Trans. 117, 682-683
[25]Tzen, J. T. C., Lai, Y. K., Chan, K. L., Huang, A. H. C. (1990) Oleosin isoforms of high and low molecular weights are present in the oil bodies of diverse seed species. Plant Physiol. 94, 1282-1289
[26]Murphy, D. J., Keen, J. N., O''Sullivan, J. N., Au, D. M. Y., Edwards, E.W., Jackson, P. J., Cummins, I., Gibbons, T., Shaw, C. H., Ryan, A. J. (1991) A class of amphipathic proteins associated with lipidstorage bodies plants. Possible similarities with animal serum apolipoproteins. Biochem. Biophys. Acta. 1088, 86-94
[27]Chuang, R. L. C., Chen, J. C. F., Chu, J., Tzen, J. T. C. (1996) Characterization of seed oil bodies and their surface oleosin isoforms from rice embryos. J. Biochem. 120, 74-81
[28]Wu, L. S. H., Wang, L. D., Chen, P. W., Chen, L. J., Tzen, J. T. C. (1998) Genomic cloning of 18kDa oleosin and detection of triacylglycerols and oleosin isoforms in maturing rice and postgerminative seedlings. J. Biochem. 123, 386-391
[29]Tai, S.S.K., Wu, L.S.H., Chen, E.C.F., Tzen, J. T. C. (1999) Molecular cloning of 11S globulin and 2S albumin, the two major seed storage proteins in sesame. Journal of Agricultural and Food Chemistry 47, 4932–4938
[30]Li, M., Smith, L. J., Clark, D. C., Wilson, R., Murphy, D. J. (1992). Secondary structures of a new class of lipid body proteins from oilseeds. J. Biol. Chem. 267, 8245-8253
[31]Huang, A. H. C. (1992). Oil bodies and oleosins in seeds. Annu. Rev. Plant Physiol. 43, 177-200
[32]Herman, E. M. (1995) Cell and molecular biology of seed oil development in Seed Development and Germination (Kigel, J. and Galili, G., eds.), pp.195-214. Marcel Dekker, New York
[33]Peng C. C., Viola S. Y. Lee., Meei-Yn Lin., Hsin-Yi Huang., Tzen, J. T. C. (2007) Minimizing the central hydrophobic domain in oleosin for the constitution of artificial oil bodies J. Agric. Food Chem. 55, 5604-5610
[34]Tzen, J. T. C., Huang, A.H. (1992) Surface structure and properties of plant seed oil bodies. J. Cell Biol. 117, 327-335
[35]Van Rooijen, G. J. H., Moloney, M. M. (1995) Plant seed oil-bodies as carriers for foreign proteins. Bio. Technology. 13, 72-77
[36]Peng, C. C., Lin, I. P., Lin, C. K., Tzen, J. T. C. (2003) Size and stability of reconstituted sesame oil bodies. Biotechnol. Prog. 19, 1623-1626
[37]Peng, C. C., Shyu, D. J., Chou, W. M., Chen, M. J., Tzen, J. T. C. (2004) Method for bacterial expression and purification of sesame cystatin via artificial oil bodies. J. Agri. Food Chem. 52, 3115-3119
[38]Chiang, C.J., Chen, H. C., Chao, Y. P., Tzen, J. T. C. (2005) Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli. J. Agric. Food Chem. 53, 4799-4804
[39]Perler, F.B., Davis, E.O., Dean, G. E., Gimble, F.S., Jack, W. E., Neff, N., Noren, C. J., Thorner, J., Belfort, M. (1994) Protein splicing elements: inteins and exteins—a definition of terms and recommended nomenclature. Nucleic Acids Res. 22, 1125-1127
[40]Chong, S., Yang, S., Paulus, H., Benner, J., Perler, F. B., Xu, M. Q. (1996) Protein splicing involving the Saccharomyces cerevisiae VMA intein: the steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system. J. Biol. Chem. 271, 22159-22168
[41]Chiang, C. J., Chen, H. C., Kuo, H. F., Chao, Y. P., Tzen, J. T. C. (2006) One-step purification of insoluble hydantoinase overproduced in Escherichia coli. Enzy Microb Tech. 39, 1152-1158
[42]曾志正. 2001.芝麻種子在生物科技上的應用.科學發展月刊. 第29卷第9期
[43]Tam, J. P., Spetzler, J. C. (1997) Multiple antigen peptide system. Methods enzymol. 289, 612-637
[44]Derman, A. I., Prinz, W. A., Belin, D., Beckwith, J.(1993) Mutation that allows disulfide bond formation in the cytoplasm of Escherichia coil., Science. 262, 1744–1747
[45]Sambrook, J., Russell, D. W. (2001) Molecular Cloning: A Laboratory Manual, 3rd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
[46]Innis, M. A., Gelfand, D. H., Sninsky, J. J., White, T. J. (1990) PCR protocols.San Diego: Academic Press.
[47]Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
[48]Polson, A. (1990) Isolation of IgY from the yolks of eggs by a chloroform polyethylene glycol procedure. Immunological Investigations 19, 253-258
[49]Schagger, H. (2006) Tricine-SDS-PAGE. Nat Protoc. 1 ,16-22
[50]黃俊儒,(2008)以人造油體蛋白質純化表達系統純化蜂王漿抗菌蛋白質- royalisin。國立中興大學生物科技學研究所碩士論文。
[51]Fassi Fehri, L., P. Sirand-Pugnet., G. Gourgues., G. Jan, H. Wróblewski., A. Blanchard. (2005) Resistance to antimicrobial peptides and stress response in Mycoplasma pulmonis. Antimicrob Agents Chemother 49, 4154-4165
[52]Béven, L., and H. Wróblewski. (1997). Effect of natural amphipathic peptides on 20 viability, membrane potential, cell shape and motility of mollicutes. Res Microbiol 148, 163-175
[53]Cole A, M., Weis, P., Diamond, G. (1997) Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J Biol Chem. 272, 12008-12013
[54]A. Speciale., R. Musumeci., G. Blandino., I. Milazzo., F. Caccamo., G. Nicoletti. (2002) Minimal inhibitory concentrations and time-kill determination of moxifloxacin against aerobic and anaerobic isolates. International Journal of antimicrobial agents 19, 111-118
[55]Jeff, C. F. Chen., Rong-Hwa Lin., Hsiou-Chen Huang., Tzen. J. T. C. (1997) Cloning, expression and isoform classification of a minor oleosin in sesame oil bodies. J. biochem, 122, 819-824
[56]Kadokura, H., Katzen, F., Beckwith, J. (2003) Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72, 111-135
[57]Peng, C. C. (2006) Application of antimicrobial peptides in biotechnology. Plant pathol.Bull. 15, 69-75
[58]Fink, J., Boman, A., Boman, H.G., Merrifield,R.B. (1989) Design, synthesis and antibacterial activity of cecropin-like model peptides. Int J Pept Protein Res. 33, 412-421
[59]Tamaoki, H., Sakakibara, S. (1991) Solution conformation of endothelin determined by means of 1H-NMR spectroscopy and distance geometry calculations. Protein Eng. 4,509-518
[60]Bulet, P., Stocklin, R., Menin, L. (2004) Antimicrobial peptides: from invertebrates to vertebrates. Immunol Rev. 198, 169-184
[61]Dimarcq, JL., Bulet, P., Hetru C., Hoffmann, J. (1998) Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers. 47, 465-477
[62]Engstrom, Y. (1999) Induction and regulation of antimicrobial peptides in Drosophila. Dev Comp Immunol. 23, 345-358
[63]Hoffmann, JA. (1995) Innate immunity of insects. Curr Opin Immunol. 7, 4-10
[64]Kimbrell, DA., Beutler, B. (2001) The evolution and genertics of innate immunity. Nat Rev Genet. 2, 256-267
[65]Otvos, Jr. L. (2000) Antibacterial peptides isolated from insects. J. Pept. Sci. 6, 497-511
[66]Salzet, M. (2001) Vertebrate innate immunity resembles a mosaic of invertebrate immune responses. Trends Immunol. 22, 285-288
[67]Cociancich, S., Ghazi, A., Hetru, C., Hoffmann, J. A., Letellier, L. (1993) Insect defensin, an antibacterial peptide, forms voltage-dependant channels in Micrococcus Luteus. J. Biol. Chem. 268, 19239-19245
[68]Okada, M., Natori, S. (1985) Ionophore activity of sarcotoxin I, a bactericidal protein of Sarcophaga peregrina. Biochem. J. 229, 453-458
[69]Christensen, B., Fink, J., Merrifield, R. B., Mauzerall, D. (1988) Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl. Acad. Sci. U.S.A. 85, 5072-5076
[70]Lockey, T. D., Ourth, D. D. (1996) Formation of pores in Escherichia coli cell membranes by a cecropin isolated from hemolymph of Heliothis virescens larvae. Eur. J. Biochem. 236, 263-271
[71]Mackler, B. F., Kreil, G. (1977) Honey bee venom melittin: correlation of nonspecific inflammatory activities with amino acid sequences. Inflammation. 2, 55~65
[72]Mangoni, M. E., Aumelas, A., Charnet, P., Roumestand, C., Chiche, L., Despaux, E., Grassy, G., Calas, B., Chavanieu, A. (1996) Change in membrane permeability induced by protegrin 1: implication of disulfide bridges for pore formation. FEBS Lett. 383, 93-98
[73]Kuzuhara, T., Nakajima, Y., Matsuyama, K., Natori, S. (1990) Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly). J Biochem (Tokyo). 107, 514-518
[74]Matsuzaki, K., Nakayama, M., Fukui, M., Otaka, A., Funakoshi, S., Fujii, N., Besshok, Miyajima, K. (1993) Role of disulfide linkages in tachyplesin-lipid interactions. Biochemistry. 32, 11704-11710
[75]Yenugu, S., Hamil, K. G., Birse, C. E., Ruben, S. M., French, F. S., Hall, S. H. (2003) Antibacterial properties of the sperm-binding proteins and peptides of human epididymis 2 (HE2) family: salt sensitivity, structural dependence and their interaction with outer and cytoplasmic membranes of Escherichia coli. Biochem J. 372, 473-483
[76]Park, J. M., Jung, J. E., Lee, B. J. (1994) Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. Biochem Biophys Res Commun. 205, 848-954
[77]Raj, P. A., Karunakaran, T., Sukumaran, D. K. (1999) Synthesis, microbicidal activity, and solution structure of the dodecapeptide from bovine neutrophils. Biopolymers. 53, 281-292


QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top
系統版面圖檔 系統版面圖檔