Abstract
We investigated the endogenous mono(ADP-ribosyl)ation of the sarcoplasmic reticulum from rabbit skeletal muscle. The autoradiogram obtained after sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the [adenylate-32P]NAD-treated sarcoplasmic reticulum vesicles revealed a major band corresponding to the MW 105 K Ca2+-dependent ATPase and other bands corresponding to proteins of MW 153, 60 and 38 K and those of 125 to 135 K range. The addition of poly L-lysine during the incubation led to an enhancement of the modification. Poly L-lysine is proving to be a pertinent tool for identifying acceptor proteins.
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