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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
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dc.contributor.author | 李德祥 | zh_TW |
dc.date.accessioned | 2021-07-01T08:20:37Z | - |
dc.date.available | 2021-07-01T08:20:37Z | - |
dc.date.issued | 1998 | |
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/76355 | - |
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(circular 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-directed mutagenesis)的技術得到兩個突變株,其中一株表現出的蛋白質(R24N),是將第24個胺基酸由精胺酸(arginine)變成了天門冬醯胺(asparagine),另外一株表現的蛋白(K45E)是將第45個胺基酸由離胺酸(lysine)變成了麩胺酸(glutamic acid)。 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天門冬醯胺,經本實驗結果證實,抗凝血的活性將降低250倍以上。根據過去的實驗,將γ-echistatin的C端,從第46個胺基酸之後切除,活性降低1.7倍,若從第45個胺基酸離胺酸之後切除,則活性降低15倍,並且我們從電腦模擬的γ-echistatin結構看出,此離胺酸與RGD sequence非常的靠近,因此推斷第45個胺基酸在活性上可能扮演重要的角色。將第45個胺基酸由原本的離胺酸變成了麩胺酸,實驗的結果指出活性大約降低2倍。因此我們推論,第45個胺基酸可能和其末端的胺基酸有協同的作用,使得γ-echistatin對於血小板上的細胞膜蛋白integrin αIlbβ3有較強的親和力,而抑制血小板的凝集。 | 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, K45E and R24N, by site directed mutagenesis. As our previous research pointed out, Lys45 might play an important role in platelet aggregation inhibition because the inhibitory potency of des(46-49)-γ-echistatin decrease 1.7-fold whereas that of des(45-49)-γ-echistatin is 15-fold less than native γ-echistatin. Furthermore, on the basis of the structural model of γ-echistatin, Lys45 is situated near the RGD loop and facing the same side of the molecule. Nevertheless, the inhibitory potency of K45E mutant is only 2-fold less than the wild type. It implies that Lys45 need to cooperate with other C-terminal residues for the effect of platelet aggregation inhibition instead of acting alone. The R24N mutant, as expected, had little activity in inhibiting platelet aggregation. | en |
dc.description.provenance | Made available in DSpace on 2021-07-01T08:20:37Z (GMT). No. of bitstreams: 0 Previous issue date: 1998 | en |
dc.description.tableofcontents | 中文摘要……………………………………………………1 Abstract……………………………………………………2 List of Abbreviations……………………………………………………3 Chapter 1: Introduction……………………………………………………4 I. Motivations of the Dissertation……………………………………………………5 II. Overview of the Coagulation Cascade……………………………………………………5 III. Overviews of Integrins……………………………………………………6 IV. Glycoprotein Ilb-Illa complex……………………………………………………7 V. AMinireview of Disintegrins……………………………………………………9 Disintegrin Structure……………………………………………………11 Disintegrins interaction with Platelet……………………………………………………13 VI. A Minireview of Echistatin……………………………………………………15 The discovery of echistatin……………………………………………………15 The synthetic and recombinant echistatin……………………………………………………15 The interaction of echistatin……………………………………………………16 The structure of echistatin……………………………………………………18 The overall structure of echistatin……………………………………………………18 The disulfide bridges of echistatin……………………………………………………18 The important of RGD loop……………………………………………………19 The importance of C-terminal domain of echistatin……………………………………………………20 Figures……………………………………………………22 Chapter 2: Synthesis of γ-Echistatin Gene……………………………………………………33 I. PCR-based strategy for γ-echistatin gene synthesis……………………………………………………34 Materials and Methods……………………………………………………35 Synthesis of oligonucleotides……………………………………………………35 Assembly of synthetic fragments by PCR……………………………………………………35 Results and Discussion……………………………………………………36 II. Cloning synthetic gene into pQE-30 vector……………………………………………………36 Materials and Methods……………………………………………………37 Ligation of the synthetic gene into pQE-30 vector……………………………………………………37 Preparation of competent M15[pREP4] cells……………………………………………………37 Transformation……………………………………………………38 Screening for positive clones……………………………………………………39 Sequence analysis……………………………………………………39 Results and Discussion……………………………………………………39 Figures……………………………………………………41 Chapter 3: The Expression of γ-Echistatin……………………………………………………47 Materials and Methods……………………………………………………48 Small-scale expression of γ-echistatin……………………………………………………48 Growing large-scale expression culture……………………………………………………48 Cell lysis and checking for cytoplasmic or periplasmic location……………………………………………………48 Purification of cytoplasmic proteins by Ni-NTA column……………………………………………………49 SDS-polyacrylamide gel electrophoresis……………………………………………………49 The process of cleavage and refolding of γ-echistatin……………………………………………………50 The modified process of cleavage and refolding of γ-echistatin……………………………………………………51 Results and Discussion……………………………………………………52 Expression of γ-echistatin……………………………………………………52 Affinity purification of 6xHis-tagged proteins……………………………………………………52 The process of cleavage and refolding of γ-echistatin……………………………………………………53 Figures……………………………………………………55 Chapter 4: Site-Directed Mutagenesis of γ-Echistatin……………………………………………………63 Materials and Methods……………………………………………………64 The megaprimer method……………………………………………………64 C irculardichroism……………………………………………………65 Results and Discussion……………………………………………………65 Site-directed mutagenesis……………………………………………………65 Expression and purification of K45E and R24N……………………………………………………66 Circular dichroism……………………………………………………66 Figures……………………………………………………67 Chapter 5: The Molecular Model of γ-Echistatin & its Mutants……………………………………………………74 Materials and Methods……………………………………………………75 Results……………………………………………………75 Figures……………………………………………………76 Chapter 6: Biological activity of γ-Echistatin……………………………………………………80 Materials and Methods……………………………………………………81 Determining protein concentration……………………………………………………81 Platelet aggregation assay……………………………………………………82 Results……………………………………………………82 Figures……………………………………………………83 Chapter 7: Discussion and Prospect……………………………………………………85 Reference……………………………………………………89 | |
dc.language.iso | zh-TW | |
dc.title | γ-Echistatin的基因合成,表現、純化及結構、功能的探討 | zh_TW |
dc.title | Study of γ-Echistatin from Scratch: Gene Synthesis, Protein Expression, Purification, Structure, and Function | en |
dc.date.schoolyear | 86-2 | |
dc.description.degree | 碩士 | |
dc.relation.page | 100 | |
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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