Jesser M, Chypre C, Hog F, Mandel P
Centre de Neurochimie du C.N.R.S., Strasbourg, France.
Biochem Biophys Res Commun. 1993 Sep 15;195(2):558-64. doi: 10.1006/bbrc.1993.2082.
A cytoplasmic poly(ADP-ribose)polymerase (PARP) was purified from mouse plasmacytoma free messenger ribonucleoprotein particles using chromatography on 3-aminobenzamide affigel-10. The purified protein showed one band at 116 kDa on SDS-polyacrylamide gel electrophoresis and shared similar antigenic sites to the nuclear PARP. An apparent Km for NAD of 100.5 +/- 6.3 microM and a Vmax of 174 +/- 40 nmoles of ADP-ribose incorporated/min/mg protein were observed. RNA was detected in the enzyme preparation and the enzymatic activity was not DNA dependent.
