[Partial purification and properties of deoxyribonucleases from eggs and liver of Xenopus laevis. Comparison with deoxyribonuclease II from bovine spleen].

Deoxyribonucleases from eggs and the liver of Xenopus laevis were partially purified by DEAE-cellulose and heparin-Sepharose affinity column chromatographies. The fractions having egg and liver DNase activities were eluted on high performance liquid chromatography through TSK gel G3000SW at the molecular weights of 41.5 and 45 kDa, respectively. The frog DNases hydrolyzed a native DNA over a heat-denatured DNA, and also formed double-strand cuts not only in linear lambda-DNA but also in closed circular pBR322DNA. The pH optimum of the DNases was 4.5-5.0 in 50 mM acetate buffer. These enzyme activities were abolished by treatment at 80 degrees C for 5 min and pH 2, 3 or 12 for 1 h. The enzymes act in such a manner as deoxyribonuclease II (from bovine spleen)-type nuclease with respect to substrate specificity, optimum pH and cation dependence.