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© 1996 Oxford University Press

research-article

Excision of DNA adducts of nitrogen mustards by bacterial and mammalian 3-methyladenine-DNA glycosylases

William B. Mattes 1, Chong-Soon Lee 2, Jacques Laval and Timothy R. O'Connor 3

Groupe Réparation des lesions radio-et chimioinduites, CNRS URA 147, Institut Gustave-Roussy 94805 Villejuif cedex, France
1Experimental Toxicology, Ciba-Geigy, Pharmaceutical Division Summit. NJ 07901, USA
2Department of Biochemistry, College of Natural Sciences, and Yeungnam University Gyongsan, 712-749. South Korea

3To whom correspondence should be addressed

Nitrogen mustards are among the DNA alkylating agents most widely used in chemotherapy. The homogeneous Escherichia coli AlKA protein (3-methyladenine DNA glycosylase II) is shown to excise damaged guanine and adenine bases from DNA modified by mechlorethamine, uracil mustard, phenylalanine mustard and chlorambucil, and less efficiently acridine mustard adducts. Homogeneous recombinant human and rat 3-methyladenine-DNA glycosylases excise adducts formed by nitrogen mustards less efficiently than the AlKA protein. In addition to the in vitro excision of adducts, the AlKA protein eliminates cytotoxic mechlorethamine adducts from DNA in vivo.


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