Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme.

@article{Moss1985ReversibilityOA,
  title={Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme.},
  author={Joel Moss and Myron K. Jacobson and Sally J. Stanley},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1985},
  volume={82 17},
  pages={5603-7}
}
Enzymes have been identified in animal tissues that catalyze the mono(ADP-ribosyl)ation of arginine and proteins. Since these NAD:arginine ADP-ribosyltransferases under physiological conditions do not appear to catalyze the degradation of the product ADP-ribose-arginine, the possibility was investigated that a different family of enzymes exists that cleaves the ADP-ribose-arginine linkage. An enzyme was identified in and partially purified from turkey erythrocytes that catalyzed the degradation… CONTINUE READING
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