期刊
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS
卷 70, 期 6, 页码 1014-1019出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2007.11.008
关键词
ADP-ribosylation; ADP-ribosylarginine hydrolase; target protein
Arginine-specific ADP-ribosylation is one of the posttranslational modifications of proteins by transferring one ADP-ribose moiety of NAD to arginine residues of target proteins. This modification, catalyzed by ADP-ribosyltransferase (Art), is reversed by ADP-ribosylarginine hydrolase (AAH). In this study, we describe a new method combining an anti-ADP-ribosylarginine antibody (alpha ADP-R-Arg Ab) and AAH for detection of the target protein of ADP-ribosylation. We have raised alpha ADP-R-Arg Ab with ADP-ribosylated histone and examined the reactivity of the antibody with proteins treated by Art and/or AAH, as well as in situ ADP-ribosylation system with mouse T cells. Our results indicate that the detection of ADP-ribosylated protein with alpha ADP-R-Arg Ab and AAH is a useful tool to explore the target proteins of ADP-ribosylation. We applied the method to search endogenously ADP-ribosylated protein in the rat, and detected possible target proteins in the skeletal muscle, which has high Art activity. (c) 2007 Elsevier B.V. All rights reserved.
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