The combination of 12–0-tetradecanoylphorbol-13-acetate and n-butyrate induced Epstein-Barr virus (EBV)-associated alkaline DNase in Raji cells. The anti-early-antigen-positive sera neutralized EBV-associated DNase activity. The enzyme activity was eluted at about 0.20 and 0.24 M KC1 from DEAE-cellulose and phosphocellulose columns, respectively. The partially purified enzyme was sensitive to (NH4)2S04 and spermine. Immunological and biochemical properties of EBV-associated DNase induced in Raji cells were similar to those of the enzyme induced in P3HR-1 cell