Abstract |
Extracts of human lymphoblastoid cells catalyzed complete release of uracil (Ura) from PBS1 DNA, which contains Ura instead of thymine as a normal component (Ura- DNA), and 3-methyladenine (3-MeAde) from DNA methylated with methyl methanesulfonate (Me- DNA). These two activities, Ura-DNA glycosylase and 3-MeAde-DNA glycosylase, differed in heat stability. Cell extracts released Ura more rapidly and 3-MeAde more slowly from alkali-denatured preparations of Ura- and Me- DNA, respectively, than from native DNA's. On incubation with reconstituted chromatins, prepared from Ura- DNA and Me- DNA, respectively, with calf thymus chromosomal protein by salt gradient dialysis, cell extracts released all the Ura but only about half of the 3-MeAde residues, although both these chromatins were degraded by micrococcal nuclease until about half of the nucleotides became acid soluble. The activities of Ura- DNA and 3-MeAde-DNA glycosylase of xeroderma pigmentosum cells were similar to those of normal cells.
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Authors | K Ishiwata, A Oikawa |
Journal | Biochimica et biophysica acta
(Biochim Biophys Acta)
Vol. 563
Issue 2
Pg. 375-84
(Jul 26 1979)
ISSN: 0006-3002 [Print] Netherlands |
PMID | 465495
(Publication Type: Journal Article)
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Chemical References |
- Chromatin
- Uracil
- DNA
- Glycoside Hydrolases
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Topics |
- Animals
- Cattle
- Cell Line
- Chromatin
- DNA
- Glycoside Hydrolases
(metabolism)
- Humans
- Kinetics
- Methylation
- Thymus Gland
- Uracil
- Xeroderma Pigmentosum
(enzymology)
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