Identification of an enzymatic activity that hydrolyzes protein-bound ADP-ribose in skeletal muscle.
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.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004226:Dithioerythritol / Q000494:pharmacology; D005459:Fluorides / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D013997:Time Factors
D011506:Proteins; D000246:Adenosine Diphosphate Ribose; D004226:Dithioerythritol; D009113:Muramidase; D008274:Magnesium; D005459:Fluorides