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.
Taniguchi
M
M
Department of Biochemistry, Shimane Medical University, Izumo 693, Japan.
Tanigawa
Y
Y
Tsuchiya
M
M
Mishima
K
K
Obara
S
S
Yamada
K
K
Shimoyama
M
M
D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002850:Chromatography, Gel; D004229:Dithiothreitol / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D011065:Poly(ADP-ribose) Polymerases / Q000302:isolation & purification* / Q000378:metabolism; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D014357:Trypsin
D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D001120:Arginine; D011065:Poly(ADP-ribose) Polymerases; D014357:Trypsin; D004229:Dithiothreitol