Purification and properties of O6-methylguanine-DNA-methyltransferase in human hepatic tissue.
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.
Yawetz
A
A
Institute for Nature Conservation Research, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel.
Katz
A
A
Waldstein
E
E
D000328:Adult; D000645:Ammonium Sulfate; D002482:Cellulose; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004247:DNA / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D006147:Guanine / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000201:enzymology*; D008297:Male; D008780:Methyltransferases / Q000302:isolation & purification*; D008970:Molecular Weight; D019853:O(6)-Methylguanine-DNA Methyltransferase
D006147:Guanine; D002482:Cellulose; D004247:DNA; C008449:O-(6)-methylguanine; D008780:Methyltransferases; D019853:O(6)-Methylguanine-DNA Methyltransferase; D000645:Ammonium Sulfate