Purification and properties of O6-methylguanine-DNA-methyltransferase in human hepatic tissue |
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Authors: | A Yawetz A Katz E Waldstein |
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Institution: | Institute for Nature Conservation Research, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel. |
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Abstract: | 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. |
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