Purification and properties of O6-methylguanine-DNA-methyltransferase in human hepatic tissue

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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.

Original languageEnglish
Pages (from-to)177-183
Number of pages7
JournalBiochemical Medicine and Metabolic Biology
Volume41
Issue number3
DOIs
StatePublished - Jun 1989

Funding

FundersFunder number
Moise and Frida Eskenasy Foundation
PHS
U.S. Department of Health and Human Services
National Cancer InstituteR01CA035895

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