Urea--DNA glycosylase in mammalian cells

Urea-DNA glycosylase, an enzyme presumed to be active in the repair of DNA damage caused by oxidizing agents, has been identified previously in Escherichia coli. This enzyme has now been shown to be present in cell extracts of calf thymus and human fibroblasts. It catalyzes the release of free urea from a double-stranded polydeoxyribonucleotide containing thymine residues fragmented by KMnO4 and NaOH treatment. The calf thymus enzyme has been 400-fold purified and largely separated from previously identified mammalian DNA glycosylases. It has a molecular weight of about 25 000 and requires no cofactors. The identity of the enzymatically released product as unsubstituted urea has been verified by its susceptibility to urease.