| Literature DB >> 6304023 |
A M Ferro, N P Higgins, B M Olivera.
Abstract
A DNA topoisomerase activity, copurifying with poly(ADP-ribose) synthetase from calf thymus, is greater than 95% inhibited if extensive poly(ADP-ribosylation) is allowed to occur. The inhibited DNA topoisomerase, which has drastically different elution properties on hydroxylapatite, can be reactivated by mild alkaline treatment. These results are consistent with a poly(ADP-ribosylation) of the DNA topoisomerase and covalent attachment of the poly(ADP-ribose) moieties to the topoisomerase by alkali-labile bonds.Entities:
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Year: 1983 PMID: 6304023
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157