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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1987-11-20
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pubmed:abstractText |
3-Methyladenine-DNA glycosylase activities have been identified in all eukaryotic cell systems studied. Some of the results from these studies are reviewed here. The enzymes possess molecular weights between 24 X 10(3) and 34 X 10(3), they have a broad pH optimum at approximately pH 8, require double-stranded DNA and act in the absence of any cofactors. The enzyme can excise several different methylated bases from DNA such as 3-methyladenine, 7-methylguanine and 3-methylguanine. The specific activity of this DNA glycosylase in mouse L-cells was found to be a function of the proliferative state of the cell. In vitro quantification of this DNA repair activity in synchronized mouse L-cells suggests that it is regulated within a defined temporal sequence prior to the onset of DNA replication. Using DNA fragments of defined sequences it was observed that the efficiency of removal of the methylated bases is sequence-dependent.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0269-3518
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
139-46
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:3477560-Animals,
pubmed-meshheading:3477560-Base Sequence,
pubmed-meshheading:3477560-Cell Cycle,
pubmed-meshheading:3477560-Cells, Cultured,
pubmed-meshheading:3477560-DNA,
pubmed-meshheading:3477560-DNA Glycosylases,
pubmed-meshheading:3477560-DNA Repair,
pubmed-meshheading:3477560-Enzyme Induction,
pubmed-meshheading:3477560-Eukaryotic Cells,
pubmed-meshheading:3477560-Humans,
pubmed-meshheading:3477560-Hydrogen-Ion Concentration,
pubmed-meshheading:3477560-Kinetics,
pubmed-meshheading:3477560-Mice,
pubmed-meshheading:3477560-Molecular Weight,
pubmed-meshheading:3477560-N-Glycosyl Hydrolases,
pubmed-meshheading:3477560-Rats
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pubmed:year |
1987
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pubmed:articleTitle |
Properties and mechanism of action of eukaryotic 3-methyladenine-DNA glycosylases.
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pubmed:affiliation |
Laboratory of Biotechnology, University of Bergen, Norway.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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