Cleavage of damaged DNA by an enzymatic activity from human fibroblasts.
An endonuclease activity isolated from normal, Xeroderma Pigmentosum and De Sanctis-Cacchione fibroblasts by DNA-cellulose chromatography has been evaluated by means of sedimentation analysis both in alkaline and neutral sucrose gradients. The partially purified enzyme is active at pH 7.5 in presence of Mg++ and cleaves UV-irradiated and alkylated DNA. Under identical experimental conditions, the enzyme is not active on untreated, depurinated and heat-denaturated DNA. The specificity on pyrimidine dimers has been further investigated to understand the mechanism of action of the enzyme.
D000478:Alkylation; D004247:DNA / Q000378:metabolism* / Q000528:radiation effects; D004260:DNA Repair; D004720:Endonucleases / Q000378:metabolism*; D005347:Fibroblasts / Q000201:enzymology*; D006801:Humans; D014466:Ultraviolet Rays; D014983:Xeroderma Pigmentosum / Q000201:enzymology
D004247:DNA; D004720:Endonucleases