Design of Probes for Sulfo-Tyrosine
碩士 === 國立臺灣大學 === 生化科學研究所 === 101 === 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, pr...
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ndltd-TW-101NTU051031092015-10-13T23:10:17Z http://ndltd.ncl.edu.tw/handle/02567505182164114245 Design of Probes for Sulfo-Tyrosine 硫酸化酪氨酸探針之設計 Yen-Min Hsu 許諺銘 碩士 國立臺灣大學 生化科學研究所 101 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. 吳世雄 2013 學位論文 ; thesis 89 en_US |
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碩士 === 國立臺灣大學 === 生化科學研究所 === 101 === 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.
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author2 |
吳世雄 |
author_facet |
吳世雄 Yen-Min Hsu 許諺銘 |
author |
Yen-Min Hsu 許諺銘 |
spellingShingle |
Yen-Min Hsu 許諺銘 Design of Probes for Sulfo-Tyrosine |
author_sort |
Yen-Min Hsu |
title |
Design of Probes for Sulfo-Tyrosine |
title_short |
Design of Probes for Sulfo-Tyrosine |
title_full |
Design of Probes for Sulfo-Tyrosine |
title_fullStr |
Design of Probes for Sulfo-Tyrosine |
title_full_unstemmed |
Design of Probes for Sulfo-Tyrosine |
title_sort |
design of probes for sulfo-tyrosine |
publishDate |
2013 |
url |
http://ndltd.ncl.edu.tw/handle/02567505182164114245 |
work_keys_str_mv |
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