ダウンロード数 : ?
ファイル
言語
英語
著者
Shibata, Tomoko Center for Integrated Research in Science, Shimane University, Faculty of Medicine, Izumo 693-8501, Japan
Yoshino, Ken-ichi
原 伸正
内容記述(抄録等)
Arginine (Arg)-specific ADP-ribosylation is one of the posttranslational modifications of proteins and is thought to play an important role in reversibly regulating functions of the target proteins in eukaryotes. However, the physiological target protein has not been established. We examined the fragmentation pattern of both ADP-ribosyl-Arg (ADP-R-Arg) and Arg-ADP-ribosylated peptides by quadrupole tandem mass spectrometry and found a specific cleavage of ADP-R-Arg into N-(ADP-ribosyl)-carbodiimide (ADP-R-carbodiimide) and ornithine. Based on this specific fragmentation pattern, we successfully identified the modification site and sequence of Arg-ADP-ribosylated peptide using a two-step collision and showed that ADP-R-carbodiimide is an excellent marker ion for precursor ion scanning of Arg-ADPribosylated peptide. We propose that a combination of the precursor ion scanning with ADP-R-carbodiimide as a marker ion and two-step collision is useful in searching for physiological target proteins of Arg-ADP-ribosylation.
主題
Arginine-specific ADP-ribosylation
Posttranslational modification
Precursor ion scanning
N-(ADP-ribosyl)-carbodiimide
Ornithine
Mass spectrometry
掲載誌名
Analytical Biochemistry
393
2
開始ページ
248
終了ページ
254
ISSN
0003-2697
発行日
2009-10-15
DOI
出版者
Elsevier
資料タイプ
学術雑誌論文
ファイル形式
PDF
著者版/出版社版
著者版
業績ID
e10622
e10605
部局
医学部
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