Molecular and immunological characterization of ADP-ribosylarginine hydrolases.

  title={Molecular and immunological characterization of ADP-ribosylarginine hydrolases.},
  author={Joel Moss and Sally J. Stanley and Maria S. Nightingale and James J. Murtagh and Luc{\'i}a Monaco and Ken-ichi Mishima and Hao Chen and Kim Williamson and Steven C Tsai},
  journal={The Journal of biological chemistry},
  volume={267 15},
Mono-ADP-ribosylation is a reversible modification of proteins with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyzing the forward and reverse reactions, respectively. Hydrolase activities were present in a variety of animal species, with the highest specific activities found in rat and mouse brain, spleen, and testis. Rat and mouse hydrolases were dithiothreitol- and Mg(2+)-dependent, whereas the bovine and guinea pig enzymes were dithiothreitol-independent. A… CONTINUE READING


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