It has been suggested that casein kinase II phosphorylates DNA topoisomerase II (topo II) in mouse FM3A cells, by comparison of phosphopeptide maps of topo II labeled in intact cells and of topo II phosphorylated by various kinases in vitro. The phosphorylation of purified topo II by casein kinase II, which attached a maximum of two phosphate groups per topo II molecule, had no effect on the activity of topo II. Dephosphorylation of purified topo II by potato acid phosphatase, which almost completely dephosphorylated the topo II, did not reduce the activity of topo II. The incubation itself, regardless of phosphorylation or dephosphorylation status, stimulated the enzyme activity in both reactions. Topo II activity was stimulated by incubation in a medium containing low concentrations of glycerol but not in that containing high concentrations of glycerol, such as the 50% in which purified topo II is stored. The stimulation of topo II activity by incubation was dependent on the concentration of topo II, requiring a relatively high concentration of topo II.

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