Removal of RNase activity from DNase by affinity chromatography on agarose coupled aminophenylphosphoryl-uridine-2' (3')-phosphate.

Severe degradation of high molecular weight RNA was shown to occur during incubation with commercially purified DNase. Most of the RNase activity could be removed by passage of the DNase through a column of agarose-coupled amino phenylphosphoryl-uridine-2' (3')-phosphate. Incubation with the treated DNase caused only minimal alteration of the sedimentation pattern of high molecular weight nuclear RNA, determined under partially denturing conditions. No impairment of DNase activity was detected.