Yawetz A, Katz A, Waldstein E
Institute for Nature Conservation Research, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel.
Biochem Med Metab Biol. 1989 Jun;41(3):177-83. doi: 10.1016/0885-4505(89)90024-8.
O6-Methylguanine-DNA-methyltransferase was partially purified from human liver. The transferase activity was purified by means of ammonium sulfate fractionation, DEAE-cellulose, Sepharose 6B, and double-strand DNA-cellulose chromatography. The native enzyme showed a molecular weight of about 44,000 as determined by gel filtration and a minimal molecular weight of 22,000 as obtained from SDS-PAGE. The native enzyme was unstable and underwent dissociation and decrease of activity in the presence of detergents.
