Mono(ADP-ribosyl)ation of Ca2+-dependent ATPase in rabbit skeletal muscle sarcoplasmic reticulum and the effect of poly L-lysine.
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.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000494:pharmacology; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D009249:NADP / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D011107:Polylysine / Q000494:pharmacology*; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000187:drug effects / Q000201:enzymology*
D010710:Phosphates; D000246:Adenosine Diphosphate Ribose; D011107:Polylysine; D009249:NADP; D001120:Arginine; D000252:Calcium-Transporting ATPases