Identification of an enzymatic activity that hydrolyzes protein-bound ADP-ribose in skeletal muscle

Biochemical and Biophysical Research Communications
Y C ChangD J Graves

Abstract

An enzymatic activity present in high-speed supernatant fluids of rat skeletal muscle was found that catalyzes the release of ADP-ribose from ADP-ribosylated-modified lysozyme. The nature of the product was proved by chromatographic studies and proton nuclear magnetic resonance spectroscopy. The enzyme activity is stimulated by Mg2+, dithioerythritol, and flouride. These results and those published earlier (Soman, G., Mickelson, J.R., Louis, C.F., and Graves, D.J. (1984) Biochem. Biophys. Res. Commun. 120, 973-980) show that ADP-ribosylation is a reversible process in skeletal muscle.

References

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Citations

Sep 1, 1994·Molecular and Cellular Biochemistry·M Tsuchiya, M Shimoyama
Sep 1, 1994·Molecular and Cellular Biochemistry·T TakadaJ Moss
Oct 2, 1992·Brain Research·M B WilliamsR S Jope
Feb 1, 1997·The International Journal of Biochemistry & Cell Biology·S TsuyamaM Tanaka
May 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·B BrüneE G Lapetina
Jan 1, 1988·Archives of Biochemistry and Biophysics·G Soman, D J Graves
Apr 15, 1991·Biochemical and Biophysical Research Communications·G SomanR W Finberg

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