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  • 03월 04일 13시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Development of improved phosphopeptide afinity tag for the enrichment of phosphopeptide

등록일
2005년 2월 17일 16시 54분 51초
접수번호
1048
발표코드
23P185포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
민혜기, 하덕찬, 이상원
고려대학교 화학과,
In signal transduction of eukaryotes, protein phosphorylation is a key event. To understand signaling processes of proteins, it is important to find their phosphorylation sites under specific condition. In this study, we developed a novel reagent not only for the enrichment of phosphopeptides, but also for identifications of phosphorylation sites. After β-elimination of a phosphate group from phosphoserine and phosphothreonine residues, an affinity tag, which has free thiol group, is reacted to the dephosphorylation sites. Primarily, a biotin tag included in the reagent permits the enrichment of phosphopeptides. The removal of acid-labile protecting group (Boc) from enriched modified peptides results in lysine residues that can be sequentially digest to generate a lysine analogs by trypsin. Such a digestion will selectively hydrolyze the phosphoproteins at the phosphorylated site. We applied this technique to analyze phosphoproteins and present the results from various applications.

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