| Summary: | 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.
|
|---|
