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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
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dc.contributor.advisor | 吳世雄 | |
dc.contributor.author | Yen-Min Hsu | en |
dc.contributor.author | 許諺銘 | zh_TW |
dc.date.accessioned | 2021-06-16T13:01:49Z | - |
dc.date.available | 2023-08-06 | |
dc.date.copyright | 2013-08-14 | |
dc.date.issued | 2013 | |
dc.date.submitted | 2013-08-07 | |
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G.: Absolute electronegativity and hardness: application to inorganic chemistry. Inorg Chem 1988, 27, 734-40. (65) Chang, D. M.: The Binding of Free Calcium-Ions in Aqueous-Solution Using Chelating-Agents, Phosphates and Poly(Acrylic Acid). J Am Oil Chem Soc 1983, 60, 618-622. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/61374 | - |
dc.description.abstract | 蛋白酪氨酸硫酸化是一種轉譯後修飾,此修飾在生理上有重要的功能。但是被發現硫酸化的蛋白量很少。目前磷酸化的酪氨酸已經有商品化的探針可以辨識被,但硫酸化的酪氨酸沒有。因此我們參考可辨識被磷酸化酪氨酸的探針,利用它結合磷酸的策略設計硫酸化酪氨酸的探針,以研究硫酸化蛋白質體。本實驗使用磷酸探針,一個磷酸探針類似物,次氮基三乙酸以及3-((2-氨基苯基)氨基甲醯基)苯甲酸與錳,鈷,鎳,銅,鋅,鈣,鍶及鋇的二價離子形成錯合物,然後測試這些錯合物與苯基磷酸或4-硝基苯基硫酸的結合力。實驗結果顯示,次氮基三乙酸/鍶或鋇可以與4-硝基苯基硫酸有結合能力,且次氮基三乙酸/鋇有較好的選擇性。根據這些結果可知鋇離子具有成為磷酸探針中心離子的潛力。因此,未來將專注在次氮基三乙酸的修飾以增加硫酸化酪氨酸探針的效能。 | zh_TW |
dc.description.abstract | Protein tyrosine O-sulfation is a post-translational modification (PTM) which was first observed in 1954. Tyrosine-sulfated proteins play the important roles in many biological processes. However, few sulfated proteins have been found by proteomics. Nowadays, protein tyrosine phosphorylation can be recognized by a commercial probe called Phos-tag but no sulf-tag was discovered and applied to sulfoproteomics. Therefore, the specific aim of this study is to design a series of sulf-tags similar to Phos-tag for the enrichment of sulfotyrosine peptides for sulfoproteomics study. We used Phos-tag, a Phos-tag analog, nitrilotriacetic acid and 3-((2-Aminophenyl)carbamoyl)benzoic acid to form complexes with Mn2+, Co2+, Ni2+, Cu2+, Zn2+ ,Ca2+, Sr2+, Ba2+, and then measured the binding ability between complexes and phenyl phosphate and 4-nitrophenyl sulfate respectively. The results showed that nitrilotriacetic acid/Sr2+ and Ba2+ could bind to 4-nitrophenyl sulfate, and nitrilotriacetic acid/Ba2+ had higher selectivity than nitrilotriacetic acid/Sr2+. On the basis of these results, Ba2+ might be the best potential metal ion to build the ideal model for pho-stag. In the future, we will focus on the modification of nitrilotriacetic acid to improve the sulf-tag. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T13:01:49Z (GMT). No. of bitstreams: 1 ntu-102-R00b46023-1.pdf: 5407825 bytes, checksum: d53e730f7f185976a515a89719c3ecc2 (MD5) Previous issue date: 2013 | en |
dc.description.tableofcontents | 1. Introduction 1
1.1 Tyrosine O-sulfation 1 1.2 Tyrosylprotein sulfotransferase (TPST) 1 1.3 Analysis and characteristics of sulfotyrosine peptides and proteins 3 1.3.1 Hydrolysis and fragmentation of sulfotyrosine 3 1.3.2 Prediction of tyrosine sulfation sites 4 1.3.3 Separation of sulfotyrosion peptides 5 1.3.4 Spectroscopic characterization of sulfotyrosine peptides 5 1.3.5 Mass spectrometry of sulfotyrosine peptides and proteins 6 1.3.6 Comparison of protein sulfation and phosphorylation 7 1.4 Phos-tag 8 1.5 Anti-sulfotyrosine antibody 9 1.6 Aim of this research 10 1.6.1 Designing the sulf-tags 10 1.6.2 Measurement of binding affinity 11 2. Material and methods 13 2.1 Instruments and general information 13 2.1.1 Instruments 13 2.1.2. Reagents 14 2.2 General methods of organic synthesis 15 2.2.1 Synthetic route 15 2.2.2 Synthetic procedure 16 2.3 ITC analysis 21 2.3.1 Materials 21 2.3.2 Methods 21 3. Results 22 3.1 ITC experiment 22 3.1.1 Titration of phosphophenol into compound 1/metal ion mixture 22 3.1.2 Titration of phosphophenol into compound 2/metal ion mixture 28 3.1.3 Titration of 4-nitrophenyl sulfate into compound 1/metal ion mixture 34 3.1.4 Titration of 4-nitrophenyl sulfate into compound 2/metal ion mixture 39 3.1.5 Titration of Ca2+, Sr2+, and Ba2+ ions into compound 9 45 3.1.6 Titration of Ca2+, Sr2+, and Ba2+ ions into compound 1 49 3.1.7 Titration of Ca2+, Sr2+, and Ba2+ ions into compound 2 52 3.1.8 Titration of Ca2+, Sr2+, and Ba2+ into nitrilotriacetic acid 55 3.1.9 Titration of phosphophenol into nitrilotriacetic acid/metal ions 59 3.1.10 Titration of 4-nitrophenyl sulfate into nitrilotriacetic acid/metal ions 63 4. Discussion 67 4.1 Binding between the complexes and phenyl phosphate or 4-nitrophenyl sulfate 67 4.2 The binding between ligands and metals 69 4.3 The binding ability of nitrilotriacetic acid and its complexes 70 4.4 Recommendation for future research 72 4.4.1 Improving the limitations of the research 72 4.4.2 Application 72 5. Reference 74 | |
dc.language.iso | en | |
dc.title | 硫酸化酪氨酸探針之設計 | zh_TW |
dc.title | Design of Probes for Sulfo-Tyrosine | en |
dc.type | Thesis | |
dc.date.schoolyear | 101-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 梁博煌,羅禮強,黃福永 | |
dc.subject.keyword | 蛋白酪氨酸硫酸化酶,等溫滴定微量熱儀, | zh_TW |
dc.subject.keyword | tyrosylprotein sulfotransferase,Tyrosine O-sulfation,Phos-tag,sulf-tag,nitrilotriacetic acid,Isothermal titration calorimetry, | en |
dc.relation.page | 89 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2013-08-07 | |
dc.contributor.author-college | 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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