TY - JOUR
T1 - Purification and properties of O6-methylguanine-DNA-methyltransferase in human hepatic tissue
AU - Yawetz, Aminadav
AU - Katz, Aviva
AU - Waldstein, Evelyn
N1 - Funding Information:
We thank Anat Faber for her devoted technical help. This research was partially supported by a grant from the Moise and Frida Eskenasy Foundation, and PHS Grant CA 35895 awarded by the National Cancer Institute, DHHS.
PY - 1989/6
Y1 - 1989/6
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/0024475333
U2 - 10.1016/0885-4505(89)90024-8
DO - 10.1016/0885-4505(89)90024-8
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AN - SCOPUS:0024475333
SN - 0885-4505
VL - 41
SP - 177
EP - 183
JO - Biochemical Medicine and Metabolic Biology
JF - Biochemical Medicine and Metabolic Biology
IS - 3
ER -