Arginine-specific ADP-ribosyltransferase from rabbit skeletal muscle sarcoplasmic reticulum is solubilized as the active form with trypsin: partial purification and characterization.

Arginine-specific ADP-ribosyltransferase from rabbit skeletal muscle sarcoplasmic reticulum was solubilized as the active form with trypsin. The enzyme was partially purified by subsequent chromatography, successively on DE-52, Con A-Sepharose and Sephadex G-75. An approximately 2,000-fold purification was achieved from the 105,000 x g supernatant of trypsin-treated membrane with a recovery of 2.8%. Dithiothreitol, which activates hen liver nuclear ADP-ribosyltransferase, inhibited the enzyme.