アフリカツメガエル(Xenopus laevis)卵及び肝由来のデオキシリボヌクレアーゼの部分精製とその性質.ウシ脾臓由来デオキシリボヌクレアーゼIIとの比較

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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 λ-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℃ for 5 min and pH 2,3 or 12 for 1h. 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.
公益社団法人日本薬学会の論文
1994-02-25