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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.
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